Priestia megaterium strains in cleaning and animal feeding

Abstract

This invention relates to a Priestia megaterium strain and mutants thereof with surprisingly advantageous properties for a beneficial cleaning effect. These Priestia strains are particularly good enzyme producers with high protease activity. The protease activity is in particular secreted protease activity and cell-bound protease activity. The invention further relates to preparations of these Priestia strains, a cleaning formulation (F) comprising the Priestia strains according to the invention, a method for cleaning an object (O) or the human or animal body (B) as well as the use of the cleaning formulation (F) in cleaning an object (O) or the human or animal body (B). It further relates to a feed or food (E) comprising the Priestia strains according to the invention and a method of feeding an animal.

Description

202400143 Foreign Filings 1 Priestia megaterium strains in cleaning and animal feeding 5 This invention relates to a Priestia megaterium strain and mutants thereof with surprisingly advantageous properties for a beneficial cleaning effect. These Priestia strains are particularly good enzyme producers with high protease activity. The protease activity is in particular secreted protease activity and cell-bound protease activity. The invention further relates to preparations of these Priestia strains, a cleaning formulation F comprising the Priestia strains according to the invention, a method for cleaning an object O 10 or the human or animal body B as well as the use of the cleaning formulation F in cleaning an object O or the human or animal body B. It further relates to a feed or food E comprising the Priestia strains according to the invention and a method of feeding an animal. Background of the Invention 15 The quest for sustainability has become a paramount concern in various industries, and the cleaning as well as the personal care sector are no exceptions. As we delve deeper into the microscopic world, the potential of utilizing microorganisms for eco-friendly solutions has become known. Among these microscopic allies, Bacillus species and others, such as Priestia species, stand out for their versatility and 20 efficiency. These robust bacteria have proven to be a treasure trove for the development of cleaning agents and the production of enzymes that pave the way for a long-lasting and sustainable approach to cleanliness. These naturally occurring bacteria produce a range of enzymes that can break down organic matter, 25 making them ideal candidates for the formulation of biodegradable and non-toxic cleaning solutions. By tapping into the inherent properties of these microorganisms, we can create products that not only clean effectively but also contribute to the well-being of our planet and its human and animal inhabitants. Products comprising microorganisms for cleaning and disinfection are described in the art. 30 E. Caselli et al., PLoS ONE 2018, 13(7):e0199616 describe probiotic-based cleaning systems for application in hospitals. Similarly, W. Stone et al., Microorganisms 2020, 8, 1726 compare the cleaning effect of a cleaning product comprising Bacillus spores on the microbiome of surfaces found in hospitals. 35 A. Spök, G. Arvanitakis, G. McClung, Food Chem Toxicol.2018, 116(Pt A), 10-19 disclose microorganisms as active ingredients in household, professional and industrial cleaning applications. US 2013 / 184196 A1 discloses an aqueous cleaning composition comprising spores of certain species of Bacillus such as Bacillus subtilis, Bacillus licheniformis, and Bacillus megaterium (= Priestia megaterium). 40 US 2023 / 220307 A1 discloses an aqueous microbial cleaning composition comprising Bacillus spores.202400143 Foreign Filings 2 WO 2008 / 146958 A1 discloses the use of Bacillus megaterium and other Bacillus species for malodor removal. 5 WO 2021 / 243324 A1 discloses microbial cleaning compositions for soft and hard surfaces comprising Bacillus, in particular Bacillus megaterium, spores with enhanced spore stability during storage and during germination after application. WO 2021 / 129998 A1 discloses probiotic strains from Bacillus, Lactobacillus, Pediococcus for degradation 10 of gluten as well as advantageous combinations of the same for gluten degradation. Bacillus megaterium DSM 33300, DSM 33356 are disclosed as possible Bacillus strains. M. Eppinger et al., Journal of Bactgeriology 2011, 193, 4199-4213 presents an analysis of the genome of Bacillus megaterium on the basis of two Bacillus megaterium strains DSM 319 and QM B1551. 15 CN 1302823 A discloses a method for producing polyhydroxyalkanoic acid by using Bacillus megaterium strain G-6. While the prior art thus provides for cleaning products comprising bacteria, there is still a need for further 20 improved cleaning agent based on Priestia with improved spectrum of activity. Detailed description of the Invention The following deposited strains were identified by screening of naturally occurring isolates and were 25 deposited at the DSMZ (“Deutsche Sammlung von Mikroorganismen und Zellkulturen”; Leibniz-Institute DSMZ-German Collection of Microorganisms and Cell Cultures, Inhoffenstraße 7B, 38124 Braunschweig, Germany) under the provisions of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purpose of Patent Procedure. 30 I. Bacillus velezensis DSM 34978 has been identified by targeted screening of naturally occurring isolates. It was isolated from the soil and has been deposited with the DSMZ on March 20, 2024 under the provisions of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purpose of Patent Procedure under the Accession Number as mentioned before in the name of Evonik Operations GmbH. 35 II. Bacillus velezensis DSM 34674 has been identified by targeted screening of naturally occurring isolates. It was isolated from the soil and has been deposited with the DSMZ on July 5, 2023 under the provisions of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purpose of Patent Procedure under the Accession 40 Number as mentioned before in the name of Evonik Operations GmbH.202400143 Foreign Filings 3 III. Bacillus licheniformis DSM 34977 has been identified by targeted screening of naturally occurring isolates. It was isolated from a bunny faeces sample and has been deposited with the DSMZ on March 20, 2024 under the provisions of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purpose of Patent 5 Procedure under the Accession Number as mentioned before in the name of Evonik Operations GmbH. IV. Priestia megaterium DSM 34980 has been identified by targeted screening of naturally occurring isolates. It was isolated from soil rifled by wild boar and has been deposited with 10 the DSMZ on March 20, 2024 under the provisions of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purpose of Patent Procedure under the Accession Number as mentioned before in the name of Evonik Operations GmbH. 15 V. Bacillus subtilis DSM 34981 has been identified by targeted screening of naturally occurring isolates. It was isolated from an environmental soil sample and has been deposited with the DSMZ on March 20, 2024 under the provisions of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purpose of Patent Procedure under the Accession Number as mentioned before in the name of Evonik Operations GmbH. 20 Surprisingly, it was found that the mentioned Bacillus / Priestia strains exhibit advantageous features as further described below. The present invention hence relates to a Priestia megaterium strain selected from the following group IV. 25 The Bacillus strains as mentioned below under numerals I, II, III, V, respectively, form part of preferred embodiments of the present invention: I. The Bacillus velezensis strain as deposited under DSM 34978 at the DSMZ and mutants thereof. II. The Bacillus velezensis strain as deposited under DSM 34674 at the DSMZ and mutants 30 thereof. III. The Bacillus licheniformis strain as deposited under DSM 34977 at the DSMZ and mutants thereof. IV. The Priestia megaterium strain as deposited under DSM 34980 at the DSMZ and mutants thereof. 35 V. The Bacillus subtilis strain as deposited under DSM 34981 at the DSMZ and mutants thereof. I. Priestia megaterium strain DSM 34980 and mutants thereof In one aspect, the present invention relates to the Priestia megaterium strain as deposited under DSM 40 34980 at the DSMZ and mutants thereof.202400143 Foreign Filings 4 “Priestia megaterium DSM 34980” strain relates to the Priestia megaterium DSM 34980 strain as deposited under DSM 34980 at the DSMZ (abbreviated as “P. megaterium DSM 34980” or “Priestia megaterium DSM 34980” or simply “DSM 34980”). 5 It was surprisingly found that Priestia megaterium DSM 34980 and mutants thereof exhibit a high expression of enzymatic activity for protease (confer point II. of the Examples) and therefore are particularly well suited to be used in cleaning formulations and in animal feeding, preferably in cleaning formulations. 10 In addition, it was surprisingly found that Priestia megaterium DSM 34980 and mutants thereof exhibit a high ability to grow on valeric acid (1000 ppm) and exhibit a high rate of metabolization of valeric acid (1000 ppm), as set forth under point IV. of the Examples. 15 Valeric acid (abbreviated as “VA”) is pentanoic acid, i.e. CH3(CH2)3COOH (CAS-No.: 109-52-4). It is preferred that the Priestia megaterium DSM 34980 strain and mutants thereof according to the invention are in a living state. 20 The cells of the Priestia megaterium DSM 34980 strain and mutants thereof according to the invention may, in particular when in a living state, be present as spores (which are dormant), as vegetative cells (which are growing), as transition state cells (which are transitioning from growth to sporulation phase) or as a combination of at least two, in particular all of these types of cells. 25 I.1 Mutants of P. megaterium DSM 34980 The mutants of P. megaterium DSM 34980 are also Priestia megaterium strains and may be obtained by any kind of method, i.e., by genetic modification methods (“GMO”) or non-GMO methods, but preferably the mutants of Priestia megaterium DSM 34980 are not genetically modified, i.e., non-GMO. It goes 30 without saying that a mutant of P. megaterium DSM 34980 is not identical with P. megaterium DSM 34980. This means that the mutants of the deposited strain of P. megaterium DSM 34980 are preferably either also naturally occurring microorganisms or spontaneous mutants of such naturally occurring microorganisms, i.e. of the deposited strains, or microorganisms which are obtained by another method which is classified as non-GMO. 35 The term “spontaneous mutant” refers to mutants that arise from naturally occurring microorganisms and / or parent strains without genetically modifying the microorganisms by applying classical gene technological and / or biotechnological methods like site-directed mutagenesis. Such spontaneous mutants may be obtained by classical methods of natural selection, such as growing the microorganisms in the202400143 Foreign Filings 5 presence of UV light and / or by applying high temperature or protoplast formation and / or in the presence of a certain antibiotic to which the parent strain is susceptible. Spontaneous mutants might further, but less preferably, be obtained by using mutagens, i.e., chemical substances which induce the formation of mutants. As formation of spontaneous mutants by using 5 mutagens is less preferred, in a preferred embodiment of the invention the spontaneous mutants and / or non-GMO mutants are obtained without the use of such mutagens. If the mutants are obtained by applying gene technological and / or biotechnological methods like site-directed mutagenesis, then preferably methods are applied which are classified as non-GMO. 10 A non-GMO method according to the invention is preferably characterized in that the method does not involve introduction of heterologous genetic information into the microorganism. In a particularly preferred embodiment of the invention the microorganisms of the invention are naturally non-occurring mutants, in particular non-GMO and / or spontaneous mutants as defined before. The microorganisms of the invention have preferably the same characteristics like the parent strain from which they are derived. 15 Preferred mutants of Priestia megaterium DSM 34980 display property (ε), more preferably display properties (ε) and (γ), even more preferably display properties (ε), (γ), and (δ) as described under point I.3. It is even more preferred that, alternatively or in addition, preferably in addition, the mutants of 20 Priestia megaterium DSM 34980 have at least characteristic (2) as follows, wherein it is even more preferred that they have at least characteristics (1) and (2) as follows: (1) a DNA sequence identity (in particular of the genomic DNA of the mutant) to the genomic DNA sequence of Priestia megaterium DSM 34980 as set forth under point I.2.1); (2) at least one, preferably at least two, more preferably at least three, even more preferably at least 25 four, even more preferably at least five, most preferably all six characteristics i., ii., iii., iv., v. and vi. as set forth under point I.2.2). I.2 Mutants of P.DSM 34980 defined by DNA sI.2.1) Sequence identity to genomic DNA 30 In a preferred embodiment of the present invention, the term “mutant of DSM 34980” refers to Priestia megaterium strains with a DNA sequence identity (in particular of the genomic DNA of the mutant) of at least 95 %, more preferred of at least 97 %, more preferred of at least 98 %, more preferred of at least 99 %, more preferred of at least 99.5 %, more preferred of at least 99.8 %, more preferred of at least 35 99.9 %, more preferred of at least 99.95 %, more preferred of at least 99.98 %, more preferred of at least 99.99 %, more preferred of at least 99.999 %, more preferred of at least 99.9999 % to the genomic DNA sequence of P. megaterium DSM 34980. The “genomic sequence of P. megaterium DSM 34980” is available / can be determined from the 40 deposited strain P. megaterium DSM 34980 by means according to the state of the art (for example, as202400143 Foreign Filings 6 summarized in the reviews by T. Hu, N. Chitnis, D. Monos, A. Dinh, Human Immunology 2021, 82, 801- 811; S. Levy & E. Boone, Cold Spring Harbor Perspectives in Medicine 2019, 9, a025791). The person skilled in the art is aware that various computer programs are available for the calculation of 5 similarity or identity between two nucleotide sequences or amino acid sequences. Preferred methods for determining the sequence identity initially generate the greatest alignment between the sequences to be compared. Computer programs for determining the identity include, but are not limited to, the GCG program package including 10 - GAP [J. Devereux, P. Haeberli, O. Smithies, Nucleic Acid Res.1984, 12, 387-395, Genetics Computer Group University of Wisconsin, Medicine (WI)], and - BLASTP, BLASTN and FASTA (S.F. Altschul, W. Gish, W. Miller, E.W. Myers, D.J. Lipman, J Mol Biol.1990, 215, 403-410; hereinafter “Altschul et al.”). The BLAST program can be obtained from the National Center for Biotechnology Information (NCBI) and from other sources (BLAST Handbook, 15 Altschul et al., NCBI NLM NIH Bethesda ND 22894). For instance, the percentage identity between two amino acid sequences can be determined by the algorithm developed by S. B. Needleman & C. D. Wunsch, J Mol Biol.1970, 48, 443-453 (hereinafter “Needleman & Wunsch”), which has been integrated into the GAP program in the GCG software 20 package, using either a BLOSUM62 matrix or a PAM250 matrix, a gap weight of 16, 14, 12, 10, 8, 6 or 4 and a length weight of 1, 2, 3, 4, 5 or 6. The person skilled in the art will recognize that the use of different parameters will lead to slightly different results, but that the percentage identity between two amino acid sequences overall will not be significantly different. The BLOSUM62 matrix is typically used applying the default settings (gap weight: 12, length weight: 1). 25 In the context of the present invention, a “sequence identity of 95 %” according to the above algorithm means “95 % homology”. The same applies to higher identities. Furthermore, in the context of the present invention, “a DNA sequence with a sequence identity of Y % to 30 the polynucleotide sequence according to SEQ ID NO: X”, means those DNA sequences that display the respective sequence identity of Y % when such sequence identity is determined by comparison of the DNA sequence over its whole length to SEQ ID NO: X over the whole length of SEQ ID NO: X. In the context of the present invention SEQ ID NO: X is, for example, selected from SEQ ID NO: 1, SEQ 35 ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29. 40202400143 Foreign Filings 7 Most preferably, the degree of identity between two nucleotide sequences is determined in the context of the present invention by the program ‘‘Needle’’ with the gap opening penalty of 10, and the gap extension penalty of 0.5. The Needle program implements the global alignment algorithm described by Needleman & Wunsch. The preferred version used in the context of this invention is the one presented by F. Madeira, 5 M. Pearce, A.R.N Tivey, P. Basutkar, J. Lee, O. Edbali, N. Madhusoodanan, A. Kolesnikov, R. Lopez, Nucleic Acids Res.2022, 50, W276–W279, Web Server issue (preferred version accessible online on Jun 1, 2024 via https: / / www.ebi.ac.uk / jdispatcher / psa / emboss_needle). I.2.2) Sequence identity to conserved DNA sequences 10 The following sequences are typical, conserved sequences of P. megaterium DSM 34980: 1. SEQ ID NO: 25: a DNA sequence coding for the 16S rRNA sequence; 2. SEQ ID NO: 26: a rpoB sequence; 3. SEQ ID NO: 27: a gyrB sequence; 15 4. SEQ ID NO: 28: a groEL sequence; 5. SEQ ID NO: 29: a yqfD sequence. In a further preferred embodiment, the mutant of DSM 34980 exhibits at least one, preferably at least two, more preferably at least three, even more preferably at least four, most preferably all five of the following 20 characteristics i. to v: i. a DNA sequence, which preferably is the DNA sequence coding for the 16S rRNA, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to 25 SEQ ID NO: 25; and / or ii. a DNA sequence, which preferably is a rpoB DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 26; and / or iii. a DNA sequence, which preferably is a gyrB DNA sequence, with a sequence identity of 30 at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 27; and / or iv. a DNA sequence, which preferably is a groEL DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 28; and / or 35 v. a DNA sequence, which preferably is a yqfD DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 29. In a most preferred embodiment, the mutant of DSM 34980 exhibits all five characteristics i., ii., iii., iv., 40 and v.202400143 Foreign Filings 8 “A DNA sequence with a certain sequence identity, in particular with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 25, 26, 27, 28, or 29” means those DNA sequences 5 that display the respective sequence identity when such sequence identity is determined by comparison of the DNA sequence over its whole length to SEQ ID NO: 25, 26, 27, 28, or 29, respectively, over the whole l of SEQ ID NO: 25, 26, 27, 28, or 29, respectively. I.3 Mutants of P. megaterium DSM 34980 defined by function 10 Priestia megaterium DSM 34980 has improved activities in terms of protease activity, as shown under point II. of the Example section. Preferably, protease activity in case of P. megaterium DSM 34980 and mutants thereof means total protease activities, i.e. secreted protease activity as well as cell-bound protease 15 In addition, Priestia megaterium DSM 34980 according to the invention has improved activities in terms of growth on 1000 ppm valeric acid and metabolization of valeric acid, as shown under point IV. of the Example section. Preferably, the ability to grow on valeric acid (1000 ppm) and the metabolization of valeric acid in case of Priestia megaterium DSM 34980 and mutants thereof is determined by the test according to Assay J. 20 In the context of the method according to the first aspect of the invention and the use according to the second aspect of the invention, those mutants of Priestia megaterium DSM 34980 are preferred that display property (ε), more preferably display properties (ε) and (γ), even more preferably display 25 properties (ε), (γ), and (δ) as follows: (γ) the mutant of Priestia megaterium DSM 34980 is able to grow on valeric acid (1000 ppm), even more preferably is able to grow on valeric acid (5000 ppm), wherein, even more preferably, the ability to grow 30 on VA (1000 ppm) as well as the ability to grow on VA (5000 ppm) is determined by the test according to Assay J, wherein “able to grow on valeric acid (1000 ppm)” means in particular that they fulfill the condition “ΓXJ;1000 ppm > 1” for xVA = 1000 ppm as determined by the test according to Assay J (point VI.5.1.4.1)” and wherein “able to grow on valeric acid (5000 ppm)” means in particular that they fulfill the condition “ΓXJ;5000 ppm> 1” for xVA= 5000 ppm as determined by the test according to Assay J (point 35 VI.5.1.4.2); (δ) the mutant of Priestia megaterium DSM 34980 has an effectiveness ΕXJ%(xVA) to reduce valeric acid [wherein xVA= 1000 ppm, preferably xVA= 5000 ppm] which is at least 85 %, preferably at least 86 %, preferably at least 87 %, preferably at least 88 %, preferably at least 89 %, preferably at least 90 %, more 40 preferably at least 91 %, more preferably at least 92 %, more preferably at least 93 %, more preferably at202400143 Foreign Filings 9 least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at least 97 %, more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more 5 preferably at least 120 % relative to the effectiveness of Priestia megaterium DSM 34980 to reduce valeric acid, wherein ΕXJ%(xVA) [wherein xVA= 1000 ppm, preferably xVA= 5000 ppm] is, in particular, determined by the test according to Assay K-II (point VI.5.2.2); (ε) the mutant of Priestia megaterium DSM 34980 has protease activity, wherein it is further preferred that 10 the mutant of Priestia megaterium DSM 34980 has a protease activity which is at least 45 %, preferably at least 50 %, preferably at least 55 %, preferably at least 60 %, preferably at least 65 %, preferably at least 70 %, preferably at least 75 %, preferably at least 78 %, preferably at least 79 %, more preferably at least 80 %, more preferably at least 81 %, more preferably at least 82 %, more preferably at least 83 %, more preferably at least 84 %, more preferably at least 85 %, more preferably at least 86 %, more 15 preferably at least 87 %, more preferably at least 88 %, more preferably at least 89 %, more preferably at least 90 %, more preferably at least 91 %, more preferably at least 92 %, more preferably at least 93 %, more preferably at least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at least 97 %, more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at 20 least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 % the protease activity of Priestia megaterium DSM 34980, wherein the protease activity of the mutant of Priestia megaterium DSM 34980 relative to the protease activity of Priestia megaterium DSM 34980 is, in particular, determined by the test according to Assay B-III (point VI.1.4). 25 I.4 Preparation In a further embodiment of the invention, the invention also relates to a preparation of Priestia megaterium DSM 34980 and / or a mutant thereof. The preparation preferably comprises at least one of Priestia megaterium DSM 34980 and mutants of Priestia megaterium DSM 34980, wherein it is even 30 more preferred that at least a part of the cells of Priestia megaterium DSM 34980 strain and mutants thereof comprised by the preparation according to the invention are in a living state. It is preferred that the preparation of Priestia megaterium DSM 34980 comprises the genomic DNA of Priestia megaterium DSM 34980. 35 It is preferred that the preparation of a mutant of Priestia megaterium DSM 34980 comprises the genomic DNA of the mutant of Priestia megaterium DSM 34980. The cells of the Priestia megaterium DSM 34980 strain and mutants thereof according to the invention 40 may, in particular when in a living state, be present, in particular in the preparation according to the202400143 Foreign Filings 10 invention, as spores (which are dormant), as vegetative cells (which are growing), as transition state cells (which are transitioning from growth to sporulation phase) or as a combination of at least two, in particular all of these types of cells. In a preferred embodiment, the preparation of the invention comprises the Priestia megaterium DSM 34980 strain and / or mutants thereof mainly or only as spores. “Mainly as 5 spores” in particular means that at least 50 %, preferably at least 50 %, preferably at least 55 %, preferably at least 60 %, preferably at least 65 %, preferably at least 70 %, preferably at least 75 %, preferably at least 80 %, preferably at least 85 %, preferably at least 90 %, preferably at least 91 %, preferably at least 92 %, preferably at least 93 %, preferably at least 94 %, preferably at least 95 %, preferably at least 96 %, preferably at least 97 %, preferably at least 98 %, preferably at least 99 %, 10 preferably at least 99.9 %, preferably at least 99.99 % of all cells of Priestia megaterium DSM 34980 strain and mutants comprised by the preparation are present as spores. Hence, in a particular embodiment, at least 50 %, preferably at least 51 %, preferably at least 55 %, 15 preferably at least 60 %, preferably at least 65 %, preferably at least 70 %, preferably at least 75 %, preferably at least 80 %, preferably at least 85 %, preferably at least 90 %, preferably at least 91 %, preferably at least 92 %, preferably at least 93 %, preferably at least 94 %, preferably at least 95 %, preferably at least 96 %, preferably at least 97 %, preferably at least 98 %, preferably at least 99 %, preferably at least 99.9 %, preferably at least 99.99 % of all cells of Priestia megaterium DSM 34980 that 20 are comprised by the preparation of Priestia megaterium DSM 34980 are present as spores. Hence, in a particular embodiment, at least 50 %, preferably at least 51 %, preferably at least 55 %, preferably at least 60 %, preferably at least 65 %, preferably at least 70 %, preferably at least 75 %, preferably at least 80 %, preferably at least 85 %, preferably at least 90 %, preferably at least 91 %, 25 preferably at least 92 %, preferably at least 93 %, preferably at least 94 %, preferably at least 95 %, preferably at least 96 %, preferably at least 97 %, preferably at least 98 %, preferably at least 99 %, preferably at least 99.9 %, preferably at least 99.99 % of all cells of a mutant of Priestia megaterium DSM 34980 that are comprised by the preparation of the mutant of Priestia megaterium DSM 34980 are present as spores. 30 Further, and although it is preferred that the cells of Priestia megaterium DSM 34980 and mutants thereof comprised by the preparation according to the invention are in a living state, in some embodiments of the present invention at least a part of the cells of Priestia megaterium DSM 34980 and / or mutants thereof comprised by the preparation may also be present in non-living, inactivated form, or as a combination of 35 living and inactivated cells, as also the non-living cells are expected to still retain protease activity. Accordingly, preparations of the Priestia megaterium DSM 34980 strain and / or mutants thereof according to the invention, may be preparations containing intact cells, preferably living cells, wherein the respective preparation may also contain inactivated cells, cell debris or mixtures thereof. 40202400143 Foreign Filings 11 Further, the preparations according to the invention may also be cell-free preparations, wherein the cell- free preparations may contain cell debris or may be free of cell debris. Particularly preferred examples according to the invention for preparations of Priestia megaterium DSM 34980 and mutants thereof are the fermentation broth, as obtained after finishing the fermentation of the cells, the supernatant of the 5 fermentation broth, which is obtained by separating all or the major part of the cells from the fermentation broth, as well as cell lysates and cell extracts, i.e. cytosol preparations, which can be obtained by breaking the microbial cells. Such preparations may also be used in concentrated or dried form, wherein the dried form has preferably a total dry matter content of at least 90 wt.-%, more preferably of at least 95 wt.-%. 10 The term “fermentation broth” according to the invention refers to the product of a cultivation of the respective bacteria, in particular Priestia megaterium DSM 34980 strain and / or mutants thereof, in a suitable fermentation medium. Methods for producing such fermentation broths are well known to those skilled in the art. The fermentation broths according to the present invention can for example be obtained 15 by culturing the strains by using the media, conditions and methods as described in US 6,060,051 A, EP 0287699 A2, US 2014 / 0010792 A1. Conventional large-scale microbial culture processes include submerged fermentation, solid state fermentation, or liquid surface culture. Typically, fermentation is carried out, until a certain cell density is reached like an optical density (OD at λ = 600 nm) of about 1 to 5, more preferably 3 to 5, even more preferably 4 to 5. The fermentation broths preferably contain cells in 20 an amount of 103to 1011CFU, more preferably in an amount of 105to 1010CFU, above all in an amount of 107to 109CFU per ml of fermentation broth. The term “fermentation broth” according to the invention refers to the direct product of the cultivation, i.e. a suspension preferably containing cells in the amount as mentioned in the previous paragraph, as well 25 as to concentrated and dried forms of such a fermentation broth, wherein the dried form (“dried fermentation broth”) preferably has a total dry matter content of at least 95 wt.-%. Drying of the preparations of the invention can be carried out by applying methods as generally known to those skilled in the art, in particular by evaporation of water, freeze-drying, lyophilization, spray drying, 30 spray granulation, fluidized bed drying, vacuum drying and combinations thereof. After drying, the dried preparations as obtained can be further worked up, in particular by grinding and / or granulation. Cell-free preparations of the respective microorganism, in particular Priestia megaterium DSM 34980 strain and / or mutants thereof, can be obtained by centrifugation, filtration and / or decantation of the 35 fermentation broth and / or by centrifugation, filtration and / or decantation of the suspension as obtained after breaking the microbial cells. Depending on the technique used, these cell-free preparations may not be completely devoid of cells, but may still comprise a smaller amount of cells, in particular up to 20 wt.-% or up to 10 wt.-% of cells. As the cells produce and secret compounds like metabolites, enzymes and / or peptides into the surrounding medium, the supernatants, extracts and lysates of the cells comprises a 40 mixture of such compounds, in particular metabolites, enzymes and / or peptides, as secreted and / or produced by the cells. In particular, the supernatants, extracts and lysates of the cells of Priestia202400143 Foreign Filings 12 megaterium DSM 34980 strain and / or mutants thereof display protease activity, preferably at least protease activity as determined by the test according to Assay A-II. Cell lysates can be prepared either directly by breaking the cells of an optionally dried fermentation broth or by breaking the cells after first separating the cells from the fermentation broth mechanically, in 5 particular by filtration, centrifugation and / or decantation. Breaking of the cells can be carried out by applying techniques as known to those of skill in the art, for example by mechanical means or by applying high pressure. Depending on the degree of force applied, a composition comprising only ruptured cells or a composition comprising a mixture of cell debris and intact 10 cells is obtained. Homogenization of the cells may be realized for example by utilizing means selected from French cell press, sonicator, homogenizer, microfluidizer, ball mill, rod mill, pebble mill, bead mill, high pressure grinding roll, vertical shaft impactor, industrial blender, high shear mixer, paddle mixer, and / or polytron homogenizer. Suitable alternatives are enzymatic and / or chemical treatment of the cells. After breaking of the cells, the cell debris and remaining cells, if any, can optionally be separated from the 15 cytosol preparation thus obtained to obtain a cell extract, i.e. a cytosol preparation, which is free of cells and cell debris. The fermentation broths of the invention, from which the cells have been removed, i.e. the cell-free supernatant and metabolites containing fractions of the fermentation broth, are also denoted as “postbiotics”, “metabiotics” or “biogenics”. 20 A further specific preparation of the invention is a preparation containing inactivated cells, i.e. cells which are not able to grow anymore. Preparations containing inactivated cells are also known as “paraprobiotics”. Such preparations can be obtained for example by heat and / or pH inactivation of the cells, preferably by heat and / or pH inactivation of a fermentation broth containing the cells. 25 Inactivation of the cells can be carried out, e.g., by heat treatment and / or by adjusting an acid or an alkaline pH. Heat inactivation of the cells is preferably carried out by increasing the temperature to between 60 °C and 80 °C and incubation for at least 30 minutes. pH inactivation at acidic pH is preferably carried out by lowering the pH to at least 3 by addition of an acid like 5 M H2SO4 and incubation for at 30 least 30 minutes, preferably at least one hour. pH inactivation at alkaline pH is preferably carried out by increasing the pH to at least 10 and incubation for at least 30 minutes, preferably at least one hour. Alternatively, inactivation of the cells may also be carried out by applying γ- or UV-irradiation. In one specific embodiment of the invention a fermentation broth is used, in which at least 90 %, more preferably at least 95 % or 99 %, in particular all bacterial cells are inactivated. Correspondingly, in this embodiment 35 of the invention a fermentation broth is used which preferably contains no viable cells, at all. The microbial preparations of the invention contain metabolites, enzymes and / or peptides as produced and / or secreted by the microorganisms of the invention, namely Priestia megaterium DSM 34980 strain and / or mutants thereof. 40202400143 Foreign Filings 13 The preparations of the invention preferably comprise an effective mixture of at least three, more preferably of at least 5, 8, 12 or 15, in particular of all metabolites of at least one microorganism of the invention. The metabolites preferably possess a molecular weight of between 400 and 100000 Dalton, more preferably of between 500 and 50000 Dalton. 5 A preparation containing an effective mixture of metabolites as contained in the microorganisms of the invention and / or as contained in the microbial preparations as mentioned before, can be obtained for example according to the methods set forth in US 6,060,051 A. The preparation can in particular be obtained by precipitating the metabolites as contained in the preparations mentioned before by using organic solvents like ethyl acetate and subsequent redissolving of the precipitated metabolites in an 10 appropriate solvent. The metabolites may subsequently be purified by size exclusion filtration that groups metabolites into different fractions based on molecular weight cut-off. The preparations of the invention can also be provided in combination with a suitable carrier, wherein the carrier is preferably an inert formulation ingredient added to improve recovery, efficacy, or physical properties and / or to aid in packaging or administration of the microorganisms or microbial preparations. 15 Such carriers may be used individually or in combination and can be added either as part of the fermentation medium, in the course of the fermentation or after the fermentation of the microorganisms has been ended. The carrier is preferably selected from anti-caking agents, antioxidants, bulking agents, binders, 20 structurants, coatings and / or protectants. Examples of useful carriers include polysaccharides (in particular starches, maltodextrins, celluloses, methylcelluloses, gums like guar gum, xanthan gum and gum arabic, wheat middlings, corn cob meal, chitosan and / or inulins), protein sources (in particular skim milk powder, sweet-whey powder, gelatine and / or soy flour), protein hydrolysates (in particular gelatine, yeast extract and / or peptones like soy peptone), peptides, sugars (in particular lactose, trehalose, 25 sucrose, dextrose and / or maltose), lipids (in particular lecithin, vegetable oils and / or mineral oils), salts (in particular sodium chloride, sodium carbonate, calcium carbonate, chalk, limestone, magnesium carbonate, sodium phosphate, calcium phosphate, magnesium phosphate and / or sodium citrate), silicates (in particular clays, zeolites, Fuller’s earth, clinoptilolite, montmorillonite, perlite, vermiculite, diatomaceous earth, talc, bentonites, kaolin clay, silica in particular precipitated silica, hydrophobic silica 30 and / or hydrophilic silica, and / or silicate salts like aluminium, magnesium and / or calcium silicate), silica gel, silica dioxide, activated carbon, lignite, magnesium and calcium oxide. I.5 Cleaning Formulation F The present invention, in a further aspect, also relates to a cleaning formulation F comprising at least one 35 of Priestia megaterium DSM 34980 and a mutant of Priestia megaterium DSM 34980 according to the invention or a preparation thereof according to the invention. Hence, the present invention, in a further aspect, also relates to a cleaning formulation F comprising at least one of Priestia megaterium DSM 34980, a mutant of Priestia megaterium DSM 34980, a preparation202400143 Foreign Filings 14 of Priestia megaterium DSM 34980, a preparation of a mutant of Priestia megaterium DSM 34980. Preparations are described above (paragraph I.4). It is preferred that the cleaning formulation F comprises at least one of Priestia megaterium DSM 34980 strain and mutants of Priestia megaterium DSM 34980 strain. 5 It is further preferred that the cleaning formulation F comprises cells of Priestia megaterium DSM 34980 strain and / or mutants thereof in a living state. The cells of the Priestia megaterium DSM 34980 strain and mutants thereof according to the invention may be present, in particular in the cleaning formulation F according to the invention, as spores (which 10 are dormant), as vegetative cells (which are growing), as transition state cells (which are transitioning from growth to sporulation phase) or as a combination of at least two, in particular all of these types of cells. In a preferred embodiment, the cleaning formulation F of the invention comprises the Priestia megaterium DSM 34980 and / or mutants thereof mainly or only as spores. “Mainly as spores” in particular means that at least 50 %, preferably at least 51 %, preferably at least 55 %, preferably at least 60 %, 15 preferably at least 65 %, preferably at least 70 %, preferably at least 75 %, preferably at least 80 %, preferably at least 85 %, preferably at least 90 %, preferably at least 91 %, preferably at least 92 %, preferably at least 93 %, preferably at least 94 %, preferably at least 95 %, preferably at least 96 %, preferably at least 97 %, preferably at least 98 %, preferably at least 99 %, preferably at least 99.9 %, preferably at least 99.99 % of all cells of Priestia megaterium DSM 34980 strain and mutants thereof 20 comprised by the cleaning formulation F are present as spores. I.5.1 Optional Ingredients of the Cleaning Formulation F The cleaning formulation F according to the present invention preferably comprises at least one of the following further ingredients. The skilled person may choose from the optional ingredients as described in 25 the following according to his knowledge and according to the intended use of the cleaning formulation F. Hence, in a preferred embodiment, cleaning formulation F further comprises at least one of surfactants, enzymes, builders, solvents, preservatives, benefit agents, polymers, bleaching systems, anti- redeposition aids, fibre protection agents, soil release agents, dye transfer inhibitors, fabric hueing 30 agents, blueing dyes, enzyme stabilizing agents like boric acid, pH-regulators, emollients, emulsifiers, thickeners / viscosity regulators / stabilizers, UV photoprotective filters, antioxidants, hydrotropes (or polyols), solids and fillers, film formers, pearlescent additives, deodorant and antiperspirant active ingredients, insect repellents, self-tanning agents, preservatives, conditioners, perfumes, dyes, odour absorbers, cosmetic active ingredients, care additives, superfatting agents, solvents, malodor removers. 35 I.5.1.1 Surfactants In a preferred embodiment, composition F comprises at least one surfactant, wherein the surfactant may be a biosurfactant SBio(rhamnolipid, sophorolipid, glucolipid) or a non-biosurfactant, preferably is a biosurfactant SBio. 40202400143 Foreign Filings 15 The at least one further surfactant may be selected from anionic surfactants, non-ionic surfactants, cationic surfactants, amphoteric surfactants, and in particular is selected from anionic surfactants, non- ionic surfactants. I.5.1.1.1 Non-ionic surfactants 5 In case the cleaning formulation F comprises at least one non-ionic surfactant, the non-ionic surfactants preferably are alkoxylated, advantageously ethoxylated, in particular primary alcohols having preferably 8 to 18 carbon atoms and on average 1 to 12 mol of ethylene oxide (“EO”) per mol of alcohol, in which the alcohol radical can be linear or branched, preferably 2-position methyl-branched, or can contain linear 10 and methyl-branched radicals in a mixture, as are customarily present in oxo alcohol radicals. In particular, however, alcohol ethoxylates with linear radicals from alcohols of native origin having 12 to 18 carbon atoms, for example from coconut, palm, tallow fat or oleyl alcohol, and on average 2 to 8 EO per mol of alcohol are preferred. The preferred ethoxylated alcohols include, for example, C12-C14-alcohols with 3 EO, 4 EO or 7 EO, C9-C11-alcohol with 7 EO, C13-C15-alcohols with 3 EO, 5 EO, 7 EO or 8 EO, 15 C12-C18-alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C12-C14-alcohol with 3 EO and C12-C18-alcohol with 7 EO. The stated degrees of ethoxylation are statistical average values which can be an integer or a fraction for a specific product. Preferred alcohol ethoxylates have a narrow homologue distribution. 20 In addition to these examples of non-ionic surfactants, it is also possible to use fatty alcohols with more than 12 EO. Examples thereof are tallow fatty alcohol with 14 EO, 25 EO, 30 EO or 40 EO. Non-ionic surfactants which contain EO and propylene oxide (“PO”) groups together in the molecule can also be used. In this connection, it is possible to use block copolymers with EO-PO block units or PO-EO block units, but also EO-PO-EO copolymers or PO-EO-PO copolymers. 25 It is of course also possible to use mixed alkoxylated non-ionic surfactants in which EO and PO units are not distributed blockwise, but randomly. Such products are obtainable as a result of the simultaneous action of ethylene oxide and propylene oxide on fatty alcohols. Furthermore, alkyl glycosides can also be used as further non-ionic surfactants. A further class of preferably used non-ionic surfactants, which are used either as the sole non-ionic 30 surfactant or in combination with other non-ionic surfactants, are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably having 1 to 4 carbon atoms in the alkyl chain, in particular fatty acid methyl esters, as are described for example in JP S58-217598 A or which are preferably prepared by the process described in WO 90 / 13533 A1. Non-ionic surfactants of the amine oxide type, for example N-cocoalkyl-N,N-dimethylamine oxide and 35 N-tallowalkyl-N,N-dihydroxyethylamine oxide, and of the fatty acid alkanolamide type may also be suitable. The amount of these non-ionic surfactants is preferably not more than that of the ethoxylated fatty alcohols, in particular not more than half thereof. Further suitable non-ionic surfactants are polyhydroxy fatty acid amides; the polyhydroxy fatty acid amides are substances which can usually be obtained by reductive amination of a reducing sugar with202400143 Foreign Filings 16 ammonia, an alkylamine or an alkanolamine and subsequent acylation with a fatty acid, a fatty acid alkyl ester or a fatty acid chloride. Further non-limiting examples of non-ionic surfactants include alcohol ethoxylates (“AE” or “AEO”), alcohol propoxylates, propoxylated fatty alcohols (“PFA”), alkoxylated fatty acid alkyl esters, such as 5 ethoxylated and / or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (“APE”), nonylphenol ethoxylates (“NPE”), alkylpolyglycosides (“APG”), alkoxylated amines, fatty acid monoethanolamides (“FAM”), fatty acid diethanolamides (“FADA”), ethoxylated fatty acid monoethanolamides (“EFAM”), polyglycerol esters, glycerol esters, propoxylated fatty acid monoethanolamides (“PFAM”), polyhydroxy alkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, “GA”, or fatty acid 10 glucamide, “FAGA”), as well as products available under the trade names “SPAN” and “TWEEN”, and combinations thereof. I.5.1.1.2 Anionic surfactants In case the cleaning formulation F comprises at least one anionic surfactant, it is preferred that these 15 anionic surfactants are of the sulphonate and sulphate type. Suitable surfactants of the sulphonate type here are preferably C9-C13-alkylbenzenesulphonates, olefine sulphonates, i.e. mixtures of alkene- and hydroxyalkanesulphonates, and also disulphonates, as are obtained, for example, from C12-C18-monoolefines with a terminal or internal double bond by sulphonation 20 with gaseous sulphur trioxide and subsequent alkaline or acidic hydrolysis of the sulphonation products. Also of suitability are alkanesulphonates which are obtained from C12-C18-alkanes, for example by sulphochlorination or sulphoxidation with subsequent hydrolysis or neutralization. Similarly, the esters of α-sulpho fatty acids (ester sulphonates), for example the α-sulphonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids, are also suitable. 25 Further suitable anionic surfactants are sulphated fatty acid glycerol esters. Fatty acid glycerol esters are to be understood as meaning the mono-, di- and triesters, and also mixtures thereof, as are obtained in the preparation by esterification of a monoglycerol with 1 to 3 mol of fatty acid or in the transesterification of triglycerides with 0.3 to 2 mol of glycerol. Preferred sulphated fatty acid glycerol esters here are the sulphation products of saturated fatty acids having 6 to 22 carbon atoms, for example of caproic acid, 30 caprylic acid, capric acid, myristic acid, lauric acid, palmitic acid, stearic acid or behenic acid. Preferred alkyl sulphates and alkenyl sulphates are the alkali metal and in particular the sodium salts of the sulphuric acid half-esters of the C12-C18-fatty alcohols, for example from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or the C10-C20-oxo alcohols and those half-esters of secondary alcohols of these chain lengths. Furthermore, preference is given to alkyl sulphates and 35 alkenyl sulphates of the specified chain length which contain a synthetic straight-chain alkyl radical prepared on a petrochemical basis, and which have an analogous degradation behaviour to the suitable compounds based on fatty chemical raw materials. From the point of view of washing, the C12-C16-alkyl sulphates and C12-C18-alkyl sulphates and also C14-C18-alkyl sulphates are preferred.2,3-Alkyl sulphates, which are prepared for example in accordance with the US 3,234,258 A or US 5,075,041 A and can be202400143 Foreign Filings 17 obtained as commercial products of the Shell Oil Company under the name DAN®, are also suitable anionic surfactants. The sulphuric acid monoesters of the straight-chain or branched C7-C20-alcohols ethoxylated with 1 to 6 mol of ethylene oxide (“EO”), such as 2-methyl-branched C9-C11-alcohols having on average 3.5 mol of 5 (“EO”) or C12-C18-fatty alcohols with 1 to 4 EO, are also suitable. On account of their high foaming behaviour, they are used in cleaning compositions only in relatively small amounts, for example in amounts of from 1 to 5 % by weight. Further suitable anionic surfactants are also the salts of alkylsulphosuccinic acid, which are also referred to as sulphosuccinates or as sulphosuccinic acid esters and constitute the monoesters and / or diesters of 10 sulphosuccinic acid with alcohols, preferably fatty alcohols and in particular ethoxylated fatty alcohols. Preferred sulphosuccinates contain C8-C18-fatty alcohol radicals or mixtures of these. Particularly preferred sulphosuccinates contain a fatty alcohol radical which is derived from ethoxylated fatty alcohols. In this connection, sulphosuccinates whose fatty alcohol radicals are derived from ethoxylated fatty alcohols with a narrow homolog distribution are particularly preferred in turn. It is likewise also possible to 15 use alkylsuccinic acid and alkenylsuccinic acid having preferably 8 to 18 carbon atoms in the alkyl chain / alkenyl chain or salts thereof. Particularly preferred anionic surfactants are soaps. Also of suitability are saturated and unsaturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, (hydrogenated) erucic 20 acid and behenic acid, and also soap mixtures derived in particular from natural fatty acids, for example coconut, palm kernel, olive oil or tallow fatty acid. The anionic surfactants including the soaps can be in the form of their sodium, potassium or ammonium salts, as well as soluble salts of organic bases, such as mono-, di- or triethanolamine. Preferably, the anionic surfactants are in the form of their sodium or potassium salts, in particular in the form of the 25 sodium salts. Non-limiting examples of anionic surfactants include sulphates and sulphonates, in particular, linear alkylbenzenesulphonates (“LAS”), isomers of LAS, branched alkylbenzenesulphonates (“BABS”), phenylalkanesulphonates, α-olefine sulphonates (“AOS”), olefine sulphonates, alkene sulphonates, 30 alkane-2,3-diylbis(sulphates), hydroxyalkanesulphonates and disulphonates, alkyl sulphates (“AS”) such as sodium dodecyl sulphate (“SDS”), fatty alcohol sulphates (“FAS”), primary alcohol sulphates (“PAS”), alcohol ethersulphates (“AES” or “AEOS” or “FES”, also known as alcohol ethoxysulphates or fatty alcohol ether sulphates) such as sodium dodecylpoly(oxyethylene) sulphate (“SLES”), secondary alkanesulphonates (“SAS”), paraffin sulphonates (“PS”), ester sulphonates, sulphonated fatty acid 35 glycerol esters, α-sulpho fatty acid methyl esters (“α-SFMe” or “SES”) including methyl ester sulphonate (“MES”), alkyl- or alkenylsuccinic acid, dodecenyl / tetradecenyl succinic acid (“DTSA”), fatty acid derivatives of amino acids, diesters and monoesters of sulfo-succinic acid or soap, and combinations thereof. 40 I.5.1.1.3 Amphotheric surfactants202400143 Foreign Filings 18 In case the cleaning formulation F comprises at least one amphotheric surfactant, it is preferred that these amphotheric surfactants are those surface-active compounds which carry at least one quaternary ammonium group and at least one -COO-- or -SO3- group in the molecule. Particularly preferred 5 amphoteric surfactants in this connection are betaine surfactants such as alkyl- or alkylamidopropylbetaines. In particular, betaines such as the N-alkyl-N,N-dimethylammonium glycinates, e.g. the cocoalkyldimethylammonium glycinate, N-acylaminopropyl-N,N-dimethylammonium glycinates, e.g. the cocoacylaminopropyldimethylammonium glycinate, the C12-C18-alkyldimethylacetobetaine, the cocoamidopropyldimethylacetobetaine, 2-alkyl-3-carboxymethyl-3-hydroxyethylimidazolines and 10 sulphobetaines having in each case 8 to 18 carbon atoms in the alkyl or acyl group, and also the cocoacylaminoethylhydroxyethylcarboxymethyl glycinate are preferred here. A particularly preferred zwitterionic surfactant is the N,N-dimethyl-N-(lauroylamidopropyl)ammoniumacetobetaine known under the INCI name Cocamidopropyl Betaine. Further suitable amphoteric surfactants are formed by the group of amphoacetates and amphodiacetates, 15 in particular, for example, coco- or laurylamphoacetates or -diacetates, the group of amphopropionates and amphodipropionates, and the group of amino acid-based surfactants such as acyl glutamates, in particular disodium cocoyl glutamate and sodium cocoyl glutamate, acyl glycinates, in particular cocoyl glycinates, and acyl sarcosinates, in particular ammonium lauroyl sarcosinate and sodium cocoyl sarcosinate. Non-limiting examples of amphoteric surfactants include betaine, alkyldimethylbetaine, 20 sulfobetaine. I.5.1.1.4 Cationic surfactants In case the cleaning formulation F comprises at least one cationic surfactant. Non-limiting examples of cationic surfactants include alklydimethylethanolamine quat (“ADMEAQ”), cetyltrimethylammonium 25 bromide (“CTAB”), dimethyldistearylammonium chloride (“DSDMAC”), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (“AQA”) compounds, and combinations thereof. I.5.1.1.5 Biosurfactants 30 It is preferred that the cleaning formulation F comprises at least one biosurfactant SBio. In the context of this invention, “biosurfactant SBio” is preferably selected from the group consisting of glucolipids, rhamnolipids, sophorolipids, even more preferably from the group of rhamnolipids. 35 Typical biosurfactants are glycolipids such as glucolipids, rhamnolipids, and sophorolipids. Such glycolipids are described in the art together with their syntheses, for example in EP 0499434 A1 (glucolipids are referred to as “glucose lipids” in this document), DE 19648439 A1, DE 19600743 A1. WO 03 / 006146 A1, US 2008 / 0213194 A1, JP H01-304034 A1, CN 1337439 A describe further methods for the synthesis of rhamnolipids. WO 03 / 002700 A1, US 4,305,961 A, US 7,556,654 B1 describe further 40 methods for the synthesis of sophorolipids.202400143 Foreign Filings 19 I.5.1.1.5.1 Glucolipid In the context of the present invention, the term “glucolipid” is in particular to be understood as referring to a structure according to formula (I), even more preferred a structure according to formula (II): 5, . In formulae (I) and (II), mGL = 3, 2, 1 or 0, preferably 1 or 0. 10 Residues R1GLand R2GLare, independently of one another, an organic radical having 2 to 24 carbon atoms, preferably 5 to 20, more preferably 7 to 15, even more preferably 7, carbon atoms, wherein preferably R1GLand R2GLare independently of one another selected from the group consisting of optionally substituted alkyl radicals with 2 to 24 preferably 5 to 20, more preferably 7 to 15, even more 15 preferably 7, carbon atoms, wherein hydroxy substituted alkyl radicals are preferred substituted alkyl radicals, optionally substituted alkenyl radicals with 2 to 24 carbon atoms, preferably 5 to 20, more preferably 7 to 15, even more preferably 7, carbon atoms, wherein hydroxy substituted alkenyl radicals are preferred 20 substituted alkenyl radicals, wherein more preferably R1GLand R2GLare independently of one another selected from the group consisting of pentenyl, heptenyl, nonenyl, undecenyl, tridecenyl and -(CH2)oCH3 where o = 1 to 23, preferably 4 to 12. Most preferably, R1GLand R2GLare each n-heptyl. 25 Distinct glucolipids for mGL = 0 are abbreviated according to the following nomenclature: “GL-CX” is understood as meaning glucolipids of the general formulae (I) or (II) in which mGL = 0 and in which the radical R1GL= (CH2)o-CH3 where o = X-4. 30 Distinct glucolipids for mGL = 1 are abbreviated according to the following nomenclature: “GL-CXCY” is understood as meaning glucolipids of the general formulae (I) or (II) in which mGL = 1 and in which one of the radicals R1GLand R2GL= (CH2)o-CH3 where o = X-4 and the remaining radical R1GLor R2GL= (CH2)o-CH3 where o = Y-4. The nomenclature used thus does not differentiate between “CXCY” and “CYCX”.202400143 Foreign Filings 20 If one of the aforementioned indices X and / or Y is provided with “:Z”, then this means that the respective radical R1GLand / or R2GL= an unbranched, unsubstituted hydrocarbon radical with X-3 or Y-3 carbon atoms having Z double bonds. The curvy bond in structure (I) [and also structures (III), (V), (VII), (IX), (XI) described hereinafter] implies 5 that the respective substituent may be axial or equatorial, preferably is equatorial. Alkyl radicals may be branched or linear. Alkenyl radicals may be branched or linear and contain at least one, preferably one to three, double 10 bonds. In those cases where structures according to formulae (I) and (II) comprise more than one residue R2GL, these residues R2GLmay be identical or different from one another. 15 In those embodiments in which cleaning formulation F comprises glucolipids, it is preferred that 1 % by weight to 30 % by weight, preferably 5 % by weight to 25 % by weight, particularly preferably 10 % by weight to 20 % by weight, of all glucolipids comprised by cleaning formulation F are GL-C8C10, where the percentages by weight refer to the sum of all of the glucolipids comprised by cleaning formulation F. 20 In those embodiments in which cleaning formulation F comprises glucolipids, it is alternatively preferred that 0.5 % by weight to 20 % by weight, preferably 3 % by weight to 17 % by weight, particularly preferably 5 % by weight to 15 % by weight, of all glucolipids comprised by cleaning formulation F are GL-C10C12:1, where the percentages by weight refer to the sum of all of the glucolipids comprised by cleaning formulation F. 25 In those embodiments in which cleaning formulation F comprises glucolipids, it is alternatively preferred that 0.5 % by weight to 20 % by weight, preferably 2 % by weight to 15 % by weight, particularly preferably 3 % by weight to 12 % by weight, of all the glucolipids comprised by cleaning formulation F are GL-C10C12, where the percentages by weight refer to the sum of all of the glucolipids comprised by 30 cleaning formulation F. In those embodiments in which cleaning formulation F comprises glucolipids, it is alternatively preferred that 1 % by weight to 30 % by weight, preferably 5 % by weight to 25 % by weight, particularly preferably 10 % 35 by weight to 20 % by weight, of all the glucolipids comprised by cleaning formulation F are GL-C8C10, 0.5 % by weight to 20 % by weight, preferably 3 % by weight to 17 % by weight, particularly preferably 5 % by weight to 15 % by weight, of all the glucolipids comprised by cleaning formulation F are GL-C10C12:1, 0.5 % by weight to 20 % by weight, preferably 2 % by weight to 15 % by weight, particularly preferably 40 3 % by weight to 12 % by weight, of all the glucolipids comprised by cleaning formulation F are GL-C10C12,202400143 Foreign Filings 21 where the percentages by weight refer to the sum of all of the glucolipids comprised by cleaning formulation F. In those embodiments in which cleaning formulation F comprises glucolipids, it is alternatively preferred 5 that 10 % by weight to 20 % by weight, of all the glucolipids comprised by cleaning formulation F are GL-C8C10, 5 % by weight to 15 % by weight, of all the glucolipids comprised by cleaning formulation F are GL-C10C12:1, 3 % by weight to 12 % by weight, of all the glucolipids comprised by cleaning formulation F are 10 GL-C10C12, where the percentages by weight refer to the sum of all of the glucolipids comprised by cleaning formulation F. Over and above this, in those embodiments in which cleaning formulation F comprises glucolipids, it is 15 alternatively preferred that 0 % by weight to 5 % by weight, preferably 0.01 % by weight to 4 % by weight, particularly preferably 0.1 % by weight to 3 % by weight, of all the glucolipids comprised by cleaning formulation F are GL-C10, where the percentages by weight refer to the sum of all of the glucolipids comprised by cleaning formulation F. 20 I.5.1.1.5.2 Rhamnolipids In the context of the present invention, the term "rhamnolipid" is in particular to be understood as referring to compounds of the general formula (III) and salts thereof, preferably compounds according to the 25 general formula (IV) and salts thereof,, . In formulae (III) and (IV), mRL = 2, 1 or 0, preferably 1 or 0. 30 nRL = 1 or 0.202400143 Foreign Filings 22 Residue R1RLand R2RLare independently of one another, an organic radical having 2 to 24 carbon atoms, preferably 5 to 13, more preferably 7 to 10, even more preferably 7, carbon atoms, wherein preferably R1RLand R2RLare independently of one another selected from the group consisting of 5 optionally substituted alkyl radicals with 2 to 24, preferably 5 to 13, more preferably 7 to 10, even more preferably 7, carbon atoms, wherein hydroxy substituted alkyl radicals are preferred substituted alkyl radicals, optionally substituted alkenyl radicals with 2 to 24, preferably 5 to 13, more preferably 7 to 10, even more preferably 7, carbon atoms, wherein hydroxy substituted alkenyl radicals are preferred substituted alkenyl 10 radicals, wherein more preferably R1RLand R2RLare independently of one another selected from the group consisting of pentenyl, heptenyl, nonenyl, undecenyl, tridecenyl and -(CH2)o-CH3 where o = 1 to 23, preferably 4 to 12. Most preferably, R1RLand R2RLare each n-heptyl. 15 If nRL = 1, the glycosidic bond between the two rhamnose units is preferably in the α-configuration. The optically active carbon atoms of the fatty acids are preferably present as R-enantiomers (e.g. (R)-3-{(R)-3- [2-O-(α-L-rhamnopyranosyl)-α-L-rhamnopyranosyl]oxydecanoyl}oxydecanoate). 20 The term ”di-rhamnolipid“ in the context of the present invention is understood to mean compounds of the general formulae (III) and (IV) or salts thereof, where nRL = 1. The term ”mono-rhamnolipid“ in the context of the present invention is understood to mean compounds of the general formulae (III) and (IV) or salts thereof, where nRL = 0. Distinct rhamnolipids are abbreviated according to the following nomenclature: 25 ”diRL-CXCY“ are understood to mean di-rhamnolipids of the general formulae (III) and (IV), in which one of the residues R1RLand R2RL= -(CH2)o-CH3 where o = X-4 and the remaining residue R1or R2= -(CH2)o-CH3 where o = Y-4. ”monoRL-CXCY“ are understood to mean mono-rhamnolipids of the general formulae (III) and (IV), in which one of the residues R1RLand R2RL= -(CH2)o-CH3 where o = X-4 and the remaining residue R1RLor 30 R2RL= -(CH2)o-CH3 where o = Y-4. The nomenclature used therefore does not distinguish between "CXCY" and "CYCX". For rhamnolipids where mRL=0, the terms “monoRL-CX” or “diRL-CX” are used accordingly. If one of the abovementioned indices X and / or Y is provided with ”:Z“, this signifies that the respective residue R1RLand / or R2RLis equal to an unbranched, unsubstituted hydrocarbon residue having X-3 or Y-3 35 carbon atoms having Z double bonds. Methods for preparing the relevant rhamnolipids are disclosed, for example, in EP 2786743 A1 and EP 2787065 A1. Rhamnolipids applicable in the context of the instant invention can also be produced by fermentation of Pseudomonas, especially Pseudomonas aeruginosa, which are preferably non genetically 40 modified cells, a technology already disclosed in the eighties, as documented e.g. in EP 0282942 A1 and DE 4127908 A1. Rhamnolipids produced in Pseudomonas aeruginosa cells which have been202400143 Foreign Filings 23 improved for higher rhamnolipid titres by genetical modification can also be used in the context of the instant invention; such cells have for example been disclosed by L. Lei, F. Zhao, S. Han, Y. Zhang, Biotechnol Lett.2020, 42, 997-1002. Rhamnolipids produced by Pseudomonas aeruginosa are commercially available from Jeneil Biotech Inc., 5 e.g. under the tradename Zonix, from Logos Technologies (technology acquired by Stepan), e.g. under the tradename NatSurFact, from Biotensidion GmbH, e.g. under the tradename Rhapynal, from AGAE technologies, e.g. under the name R90, R95, R95Md, R95Dd, from Locus Bio-Energy Solutions and from Shanghai Yusheng Industry Co. Ltd., e.g. under the tradename Bio-201 Glycolipids. 10 In those embodiments in which cleaning formulation F comprises rhamnolipids, it is preferred that these rhamnolipids comprised by cleaning formulation F are mixtures of mono-rhamnolipids and di- rhamnolipids, wherein even more preferably the ratio of the weight of all mono-rhamnolipids comprised by cleaning formulation F to the weight of all di-rhamnolipids comprised by cleaning formulation F is in the range of from 9 : 1 to 1 : 9, preferably of from 8 : 2 to 2 : 8, more preferably of from 7 : 3 to 3 : 7, more 15 preferred of from 6 : 4 to 4 : 6, most preferred is 1 : 1. Mono-rhamnolipids are compounds according to formula (III), preferably (IV), wherein nRL = 0. Di-rhamnolipids are compounds according to formula (III), preferably (IV), wherein nRL = 1. 20 In those embodiments in which cleaning formulation F comprises rhamnolipids, it is preferred that 56 % by weight to 95 % by weight, preferably 60 % by weight to 80 % by weight, particularly preferably 66 % by weight to 70 % by weight, of all rhamnolipids comprised by cleaning formulation F are diRL-C10C10, where the percentages by weight refer to the sum of all of the rhamnolipids comprised by cleaning formulation F. 25 In those embodiments in which cleaning formulation F comprises rhamnolipids, it is alternatively preferred that 0.5 % by weight to 15 % by weight, preferably 3 % by weight to 12 % by weight, particularly preferably 5 % by weight to 10 % by weight, of all rhamnolipids comprised by cleaning formulation F are diRL-C10C12:1, where the percentages by weight refer to the sum of all of the rhamnolipids comprised by 30 cleaning formulation F. In those embodiments in which cleaning formulation F comprises rhamnolipids, it is alternatively preferred that 0.5 to 25 % by weight, preferably 3 % by weight to 15 % by weight, particularly preferably 5 % by weight to 12 % by weight, of all rhamnolipids comprised by cleaning formulation F are diRL-C10C12, 35 where the percentages by weight refer to the sum of all of the rhamnolipids comprised by cleaning formulation F. In those embodiments in which cleaning formulation F comprises rhamnolipids, it is alternatively preferred that 0.1 % by weight to 25 % by weight, preferably 2 % by weight to 10 % by weight, particularly 40 preferably 4 % by weight to 8 % by weight, of all rhamnolipids comprised by cleaning formulation F are202400143 Foreign Filings 24 diRL-C8C10, where the percentages by weight refer to the sum of all of the rhamnolipids comprised by cleaning formulation F. In those embodiments in which cleaning formulation F comprises rhamnolipids, it is even further preferred 5 that 0.1 % by weight to 5 % by weight, preferably 0.5 % by weight to 3 % by weight, particularly preferably 0.5 % by weight to 2 % by weight, of all rhamnolipids comprised by cleaning formulation F are monoRL-C8C10 and / or, preferably and, 0.1 % by weight to 5 % by weight, preferably 0.5 % by weight to 3 % by weight, particularly preferably 10 0.5 % by weight to 2 % by weight, of all rhamnolipids comprised by cleaning formulation F are monoRL-C10C10, where the percentages by weight refer to the sum of all of the rhamnolipids comprised by cleaning formulation F. In those embodiments in which cleaning formulation F comprises rhamnolipids, it is alternatively preferred 15 that 10 % by weight to 30 % by weight, preferably 20 % by weight to 30 % by weight, particularly preferably 25 % by weight to 30 % by weight, of all rhamnolipids comprised by cleaning formulation F are monoRL-C10C10, where the percentages by weight refer to the sum of all of the rhamnolipids comprised by cleaning formulation F. 20 In those embodiments in which cleaning formulation F comprises rhamnolipids, it is alternatively preferred that 10 % by weight to 30 % by weight, preferably 12 % by weight to 25 % by weight, particularly preferably 15 % by weight to 20 % by weight, of all rhamnolipids comprised by cleaning formulation F are diRL-C10C10, where the percentages by weight refer to the sum of all of the rhamnolipids comprised by cleaning formulation F. 25 In those embodiments in which cleaning formulation F comprises rhamnolipids, it is alternatively preferred that 10 % by weight to 30 % by weight, preferably 12 % by weight to 25 % by weight, particularly preferably 15 % by weight to 20 % by weight, of all rhamnolipids comprised by cleaning formulation F are monoRL-C8C10, where the percentages by weight refer to the sum of all of the rhamnolipids comprised 30 by cleaning formulation F. In those embodiments in which cleaning formulation F comprises rhamnolipids, it is alternatively preferred that 3 % by weight to 25 % by weight, preferably 5 % by weight to 20 % by weight, particularly preferably 10 % by weight to 15 % by weight, of all rhamnolipids comprised by cleaning formulation F are 35 monoRL-C10C12:1, where the percentages by weight refer to the sum of all of the rhamnolipids comprised by cleaning formulation F. In those embodiments in which cleaning formulation F comprises rhamnolipids, it is alternatively preferred that 1 % by weight to 15 % by weight, preferably 2 % by weight to 10 % by weight, particularly preferably 40 3 % by weight to 8 % by weight, of all rhamnolipids comprised by cleaning formulation F are202400143 Foreign Filings 25 diRL-C10C12, where the percentages by weight refer to the sum of all of the rhamnolipids comprised by cleaning formulation F. I.5.1.1.5.3 Sophorolipids 5 In the context of the present invention, the term “sophorolipids” is in particular to be understood as referring to compounds of the general formulae (V), (VII) and salts thereof, preferably compounds of the general formulae (VI), (VIII) and salts thereof:1015 Formulae (V), (VI) represent the acid form, Formulae (VII), (VIII) represent the lactone form. In formulae (V), (VI), nSL = 4, 3, 2, 1 or 0, preferably nSL = 1 or 0.202400143 Foreign Filings 26 In formulae (V), (VI), (VII), and (VIII), R1SL= H or -CO-CH3, R2SL= H or -CO-CH3, R3SL= a divalent organic moiety which comprises 6 to 32 carbon atoms, preferably 12 to 20, more 5 preferably 14 to 16, most preferably 15 carbon atoms. In those cases where a compound according to one of formulae (V), (VI), comprises more than one residue R2SL, these residues R2SLmay be the same or different. 10 R3SLpreferably is an optionally substituted, divalent hydrocarbon moiety comprising 6 to 32 carbon atoms, wherein hydroxy substituted hydrocarbon moieties are preferred as substituted hydrocarbon moieties. R3SLmore preferably is selected from the group consisting of • optionally substituted alkylene radicals with 6 to 32, preferably 12 to 20, more preferably 14 to 15 16, most preferably 15, carbon atoms, wherein hydroxy-substituted alkylene radicals are preferred substituted alkylene radicals, and wherein it is preferred that the optionally substituted alkylene radicals are unbranched, • optionally substituted alkenylene radicals with 6 to 32, preferably 12 to 20, more preferably 14 to 16, most preferably 15, carbon atoms, wherein hydroxy-substituted alkenylene radicals are 20 preferred substituted alkenylene radicals, and wherein it is preferred that the optionally substituted alkenylene radicals are unbranched, and wherein it is preferred that the optionally substituted alkenylene radicals comprise one to three double or triple bonds. R3SLeven more preferably is selected from the group consisting of 25 • unbranched or branched, preferably unbranched, alkylene radicals with 6 to 32, preferably 12 to 20, more preferably 14 to 16, most preferably 15, carbon atoms, • unbranched or branched, preferably unbranched, alkylene radicals with 6 to 32 preferably 12 to 20, more preferably 14 to 16, most preferably 15, carbon atoms carrying at least one hydroxy group, preferably one hydroxy group, 30 • unbranched or branched, preferably unbranched, alkenylene radicals with 6 to 32, preferably 12 to 20, more preferably 14 to 16, most preferably 15, carbon atoms, wherein the alkenylene radicals preferably comprise one to three double or triple bonds, wherein the alkenylene radicals more preferably comprise one to three double bonds, even more preferably one double bond, 35 • unbranched or branched, preferably unbranched, alkenylene radicals with 6 to 32, preferably 12 to 20, more preferably 14 to 16, most preferably 15, carbon atoms carrying at least one hydroxy group, preferably one hydroxy group, wherein the alkenylene radicals preferably comprise one to three double or triple bonds, wherein the alkenylene radicals more preferably comprise one to three double bonds, even more preferably one double bond. 40 R4SL= H, CH3 or a monovalent organic radical which comprises 2 to 10 carbon atoms.202400143 Foreign Filings 27 R4SLis preferably selected from the group consisting of • H, • CH3, 5 • optionally substituted alkyl radicals with 2 to 10 carbon atoms, wherein hydroxy-substituted alkyl radicals are preferred substituted alkyl radicals, and wherein it is preferred that the optionally substituted alkyl radicals are unbranched, • optionally substituted alkenyl radicals with 2 to 10 carbon atoms, wherein hydroxy-substituted alkenyl radicals are preferred substituted alkenyl radicals, and wherein it is preferred that the 10 optionally substituted alkenyl radicals are unbranched, and wherein it is preferred that the optionally substituted alkenyl radicals comprise one to three double or triple bonds. R4SLis more preferably selected from the group consisting of • H, 15 • CH3, • unbranched or branched, preferably unbranched, alkyl radicals with 2 to 10 carbon atoms, • unbranched or branched, preferably unbranched, alkyl radicals with 2 to 10 carbon atoms carrying at least one hydroxy group, preferably one hydroxy group, • unbranched or branched, preferably unbranched, alkenyl radicals with 2 to 10 carbon atoms, 20 wherein the alkenyl radicals preferably comprise one to three double or triple bonds, wherein the alkenyl radicals more preferably comprise one to three double bonds, even more preferably one double bond, • unbranched or branched, preferably unbranched, alkenyl radicals with 2 to 10 carbon atoms carrying at least one hydroxy group, preferably one hydroxy group, wherein the alkenyl radicals 25 preferably comprise one to three double or triple bonds, wherein the alkenyl radicals more preferably comprise one to three double bonds, even more preferably one double bond. R4SLis most preferably selected from the group consisting of H, Methyl, Ethyl, even more preferably Methyl. 30 In an even more preferred embodiment, the term “sophorolipids” is to be understood as referring to compounds of the general formulae (IX), (XI) and salts thereof, preferably compounds of the general formulae (X), (XII) and salts thereof:202400143 Foreign Filings 28Formulae (IX), (X) represent the acid form. Formulae (XI), (XII) represent the lactone form. 5 nSL, R1SL, R2SL, R4SLhave the same meaning as described for formulae (V), (VII), (VI), (VIII). Sophorolipids may be used in accordance with the invention in their acid form or their lactone form. In those embodiments in which cleaning formulation F comprises sophorolipids, it is preferred that these sophorolipids comprised by cleaning formulation F are mixtures of the acid and the lactone form, wherein 10 even more preferably the ratio of the weight of all sophorolipids in the lactone form comprised by cleaning formulation F to the weight of all sophorolipids in the acid form comprised by cleaning formulation F is in the range of from 20 : 80 to 80 : 20, especially preferably in the range of from 30 : 70 to 40 : 60. To determine the content of sophorolipids in the acid or lactone form in a formulation, refer to 15 EP 1411111 B1, page 8, paragraph

[0053] . Sophorolipids may be obtained as described in EP 1411111 A1, paragraphs

[0021] ,

[0022] . Cleaning solution F may also comprise derivatives of sophorolipids such as esters of glycerol which are esterified with sophorolipids (mono-, di-, and triesters of sophorolipids with glycerol) and optionally also 20 fatty acids. Cleaning solution F may therefore comprise derivatives of sophorolipids such as those described in EP 3034613 A1 or EP 4317448 A1.202400143 Foreign Filings 29 I.5.1.2 Enzymes As stated above, cleaning formulation F comprises Priestia megaterium DSM 34980 strain and / or mutants thereof. Priestia megaterium DSM 34980 strain and / or mutants thereof have superior properties 5 in terms of protease activity. This is an enzymatic activity. In addition, the cleaning formulation F may comprise enzymes with similar or different activities. In a preferred embodiment, the cleaning formulation F also comprises at least one enzyme E. 10 In those embodiments where the cleaning formulation F comprises at least one enzyme E, it is further preferred that the enzyme E is selected from the group consisting of protease, amylase, cellulase, mannanase, lipase, cutinase, pectate lyase, peroxidase, oxidase, laccase. It is even more preferred that the at least one enzyme E is selected from the group consisting of protease, amylase, lipase, mannanase. Most preferred, the at least one enzyme E is a lipase. 15 In case the cleaning formulation F comprises at least one enzyme E, it is preferred that the amount of all enzymes E comprised by the cleaning formulation F is in the range of 0.1 to 4 wt.-% per the total weight of cleaning formulation F. The at least one enzyme E may be included in the cleaning formulation F by adding separate additives 20 (“detergent additives”) containing one or more enzymes, or by adding a combined additive comprising all enzymes E comprised by the cleaning formulation F. Such a detergent additive as contemplated herein, i.e., a separate additive or a combined additive, can be formulated, for example, as a granulate, liquid, slurry, etc. Preferred detergent additive formulations are granulates, in particular non-dusting granulates, liquids, in particular stabilized liquids, or slurries. 25 Non-dusting granulates may be produced, e.g., as disclosed in US 4,106,991 A and US 4,661,452 A and may optionally be coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, “PEG”) with mean molar weights of from about 1000 to about 20000 g / mol; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units per molecule; 30 ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms per molecule and in which there are 15 to 80 ethylene oxide units per molecule; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluid bed techniques are given in GB 1,483,591 A. Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid or boric acid according 35 to established methods. Protected enzymes may be prepared according to the method disclosed in EP 0238216 A1. I.5.1.2.1 Cellulases202400143 Foreign Filings 30 In those embodiments where the cleaning formulation F comprises at least one cellulase, suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g., the fungal cellulases produced from Humicola insolens, 5 Myceliophthora thermophila and Fusarium oxysporum disclosed in US 4,435,307 A, US 5,648,263 A, US 5,691,178 A, US 5,776,757 A and WO 89 / 09259 A1. Especially suitable cellulases are the alkaline or neutral cellulases having color care benefits. Examples of such cellulases are cellulases described in EP 0495257 A1, WO 91 / 17243 A1, WO 96 / 11262 A1, WO 96 / 29397 A1, WO 98 / 08940 A1. Other examples are cellulase variants such as those described in 10 WO 94 / 07998 A1, WO 91 / 17244 A1, US 5,457,046 A, US 5,686,593 A, US 5,763,254 A, WO 95 / 24471 A1, WO 98 / 12307 A1 and WO 99 / 01544 A1. Example of cellulases exhibiting endo-β-1,4-glucanase activity (EC 3.2.1.4) are those described in WO 02 / 099091 A2. 15 Commercially available cellulases include Celluzyme™, and Carezyme™ (Novozymes A / S), Clazinase™, and Puradax HA™ (Genencor International Inc.), and KAC-500(B)™ (Kao Corporation). I.5.1.2.2 Proteases 20 In those embodiments where the cleaning formulation F comprises at least one protease (in addition to the protease activity exerted by Priestia megaterium DSM 34980 and mutants thereof), suitable proteases include those of bacterial, fungal, plant, viral or animal origin e.g. vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. A serine protease may for example be of the 25 S1 family, such as trypsin, or the S8 family such as subtilisin. A metalloproteases may for example be a thermolysin from e.g. family M4 or other metalloprotease such as those from M5, M7 or M8 families. The term “subtilases” refers to a sub-group of serine protease according to R.J. Siezen, W.M. de Vos, J.A.M. Leunissen, B.W. Dijkstra, Protein Engineering, Design and Selection 1991, 4, 719-737 and R.J. Siezen & J.A. Leunissen, Protein Science 1997, 6, 501-523. Serine proteases are a subgroup of 30 proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate. The subtilases may be divided into 6 sub-divisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family. Examples of subtilases are those derived from Bacillus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in: US 7,262,042 B2 and 35 WO 2009 / 021867 A2, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN′, subtilisin 309, subtilisin 147 and subtilisin 168 described in WO 89 / 06279 A1 and protease PD138 described in WO 93 / 18140 A1. Other useful proteases may be those described in WO 2019 / 105675 A1, WO 01 / 016285 A2, and WO 02 / 016547 A2. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89 / 06270 A1,202400143 Foreign Filings 31 WO 94 / 25583 A1 and WO 2005 / 040372 A1, and the chymotrypsin proteases derived from Cellumonas described in WO 2005 / 052161 A2 and WO 2005 / 052146 A2. A further preferred protease is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO 95 / 23221 A1, and variants thereof which are described in WO 92 / 21760 A2, 5 WO 95 / 23221 A1, EP 1921147 A2, and EP 1921148 A2. Examples of metalloproteases are the neutral metalloprotease as described in WO 2007 / 044993 A2 (Genencor Int.) such as those derived from Bacillus amyloliquefaciens. Examples of useful proteases are the variants described in: WO 92 / 19729 A1, WO 96 / 34946 A1, WO 98 / 20115 A1, WO 98 / 20116 A1, WO 99 / 11768 A1, WO 01 / 44452 A1, WO 03 / 006602 A2, 10 WO 2004 / 03186 A2, WO 2004 / 041979 A2, WO 2007 / 006305 A1, WO 2011 / 036263 A1, WO 2011 / 036264 A1. Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Liquanase® 2.5 L, Ovozyme®, Coronase, Coronase® Ultra, 15 Neutrase®, Everlase®, and Esperase® (Novozymes A / S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect Prime®, Eraser®, Purafect MA®, Purafect Ox®, Purafect OxP®, Puramax®, Properase®, Ultimase®, FN2®, FN3®, FN4®, Excellase®, Opticlean®, and Optimase® (Danisco / DuPont), Axapem™ (Gist-Brocases N.V.), BLAP (sequence shown in Figure 29 of US 5,352,604 A) and variants thereof (Henkel AG) and KAP (Bacillus alkalophilus subtilisin) from Kao. 20 A protease preferably comprised in the composition according to the instant invention is Liquanase® 2.5 L. In a preferred embodiments, the proteases comprised by cleaning formulation F are stabilized by biosurfactants SBio such as rhamnolipids, as described in US 2018 / 023040 A1. 25 I.5.1.2.3 Lipases and cutinases In those embodiments where cleaning formulation F comprises at least one of lipase, cutinase, suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from 30 T. lanuginosus (previously named Humicola lanuginosa) as described in EP 0258068 A2 and EP 0305216 A1, cutinase from Humicola, e.g. H. insolens (WO 96 / 13580 A1), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP 0218272 A1), P. cepacia (EP 0331376 A2), P. sp. strain SD705 (US 5,827,718 A & US 5,942,431 A), P. wisconsinensis (WO 96 / 12012 A1), GDSL-type Streptomyces lipases 35 (WO 2010 / 065455 A2), cutinase from Magnaporthe grisea (WO 2010 / 107560 A2), cutinase from Pseudomonas mendocina (US 5,389,536 A), lipase from Thermobifida fusca (WO 2011 / 084412 A1), Geobacillus stearothermophilus lipase (WO 2011 / 084417 A1), lipase from Bacillus subtilis (WO 2011 / 084599 A1), and lipase from Streptomyces griseus (WO 2011 / 150157 A2) and S. pristinaespiralis (WO 2012 / 137147 A1).202400143 Foreign Filings 32 Other examples are lipase variants such as those described in EP 0407225 A1, WO 92 / 05249 A1, WO 94 / 01541 A1, WO 94 / 25578 A1, WO 95 / 14783 A1, WO 95 / 30744 A2, WO 95 / 35381 A1, WO 95 / 22615 A1, WO 96 / 00292 A1, WO 97 / 04079 A1, WO 97 / 07202 A1, WO 00 / 34450 A1, WO 00 / 60063 A1, WO 01 / 92502 A1, WO 2007 / 87508 A2, CN 104031899 A, and WO 2009 / 109500 A1. 5 Preferred commercial lipase products include Lipolase™, Lipex™; Lipolex™, Lipex™ 100 L Evity and Lipoclean™ (Novozymes A / S), Lumafast (originally from Genencor) and Lipomax (originally from Gist- Brocades). Still other examples are lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO 2010 / 111143 A2), acyltransferase 10 from Mycobacterium smegmatis (WO 2005 / 56782 A2), perhydrolases from the CE 7 family (WO 2009 / 67279 A1), and variants of the Mycobacterium smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd. (WO 2010 / 100028 A2). I.5.1.2.4 Amylases 15 In those embodiments where cleaning formulation F comprises at least one amylase, suitable amylases which can be used herein may be an α-amylase or a glucoamylase and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, α-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail 20 in GB 1,296,839 A. Suitable amylases include amylases having SEQ ID NO: 3 in WO 95 / 10603 A1 or variants having about 90 % sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94 / 02597 A1, WO 94 / 18314 A1, WO 97 / 43424 A1, and SEQ ID NO: 4 of WO 99 / 19467 A1. Different suitable amylases include amylases having SEQ ID NO: 6 in WO 02 / 10355 A2 or variants 25 thereof having about 90 % sequence identity thereto. Other amylases which are suitable are hybrid α-amylase comprising residues 1-33 of the α-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 A2 and residues 36-483 of the B. licheniformis α-amylase shown in SEQ ID NO: 4 of WO 2006 / 066594 A2 or variants having about 90 % sequence identity thereof. 30 Further amylases which are suitable are amylases having SEQ ID NO: 6 in WO 99 / 019467 A1 or variants thereof having about 90 % sequence identity to SEQ ID NO: 6. Additional amylases which can be used are those having SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 of WO 96 / 23873 A1 or variants thereof having 90 % sequence identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7. 35 Other amylases which can be used are amylases having SEQ ID NO: 2 of WO 2008 / 153815 A1, SEQ ID NO: 10 in WO 01 / 66712 A2 or variants thereof having about 90 % sequence identity to SEQ ID NO: 2 of WO 2008 / 153815 A1 or about 90 % sequence identity to SEQ ID NO: 10 in WO 01 / 66712 A2. Further suitable amylases are amylases having SEQ ID NO: 2 of WO 2009 / 061380 A2 or variants having 40 about 90 % sequence identity to SEQ ID NO: 2 thereof.202400143 Foreign Filings 33 Other suitable amylases are the α-amylase having SEQ ID NO: 12 in WO 01 / 66712 A2 or a variant having at least about 90 % sequence identity to SEQ ID NO: 12. Other examples are amylase variants such as those described in WO 2011 / 098531 A1, WO 2013 / 001078 A1 and WO 2013 / 001087 A2. 5 Commercially available amylases are Amplify™ Prime 100 L, Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natalase™, Liquozyme X and BAN™ (from Novozymes A / S), and Rapidase™, Purastar™ / Effectenz™, Powerase and Preferenz S100 (from Genencor International Inc. / DuPont). I.5.1.2.5 Peroxidases / oxidases 10 In those embodiments where cleaning formulation F comprises at least one peroxidase or oxidase, suitable peroxidases / oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g., from C. cinereus, and variants thereof as those described in WO 93 / 24618 A1, 15 WO 95 / 10602 A1, and WO 98 / 15257 A1. Commercially available peroxidases include Guardzyme™ (Novozymes A / S). I.5.1.2.6 Mannanases In those embodiments where cleaning formulation F comprises at least one mannanase, mannanases 20 which are particularly preferred according to the invention are mannanases which are sold, for example, under the trade names Mannaway® by the company Novozymes or Purabrite® by the company Genencor. A mannanase preferably comprised in the cleaning formulation F is Mannaway® 4.0 L. I.5.1.3 Builders 25 Cleaning formulation F may also comprise at least one builder BZ. This is especially useful in those cases where cleaning formulation F is applied as laundry composition. In those embodiments where cleaning formulation F comprises at least one builder BZ, the amount of all builders BZin cleaning formulation F is preferably between 0.1 wt.-% to 10 wt.-%, preferably 1 wt.-% to 30 7 wt.-%, relative to the total weight of cleaning formulation F. The builder BZ may particularly be a chelating agent that forms water-soluble complexes with calcium and magnesium. Non-limiting examples of builders BZinclude zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (“STP” or “STPP”), carbonates such as sodium carbonate, 35 soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Hoechst), ethanolamines such as 2-aminoethan-1-ol (“MEA”), diethanolamine (“DEA”, also known as iminodiethanol), triethanolamine (“TEA”, also known as 2,2’,2’’-nitrilotriethanol), and carboxymethyl inulin (“CMI”), and combinations thereof.202400143 Foreign Filings 34 Non-limiting examples of builders BZinclude homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (“PAA”) or copoly(acrylic acid / maleic acid) (“PAA / PMA”). Further non-limiting examples of builders BZinclude polyaspartic acids and polyglutamic acids and their salts, citrates, ascorbic acid, chelators such as aminocarboxylates, aminopolycarboxylates, like N,N-dicarboxymethyl 5 glutamic acid and methylglycine N,N-diacetic acid, and phosphonates, and alkyl- or alkenylsuccinic acid. Additional specific examples of builders BZinclude 2,2’,2’’-nitrilotriacetic acid (“NTA”), ethylenediaminetetraacetic acid (“EDTA”), diethylenetriaminepentaacetic acid (“DTPA”), iminodisuccinic acid (“IDS”), ethylenediamine-N,N’-disuccinic acid (“EDDS”), glutamic acid-N,N-diacetic acid (“GLDA”), 1-hydroxyethane-1,1-diphosphonic acid (“HEDP”), ethylenediaminetetra-(methylenephosphonic acid) 10 (“EDTMPA”), diethylenetriaminepentakis(methylenephosphonic acid) (“DTPMPA” or “DTMPA”), N-(2-hydroxyethyl)iminodiacetic acid (“EDG”), aspartic acid-N-monoacetic acid (“ASMA”), aspartic acid- N,N-diacetic acid (“ASDA”), aspartic acid-N-monopropionic acid (“ASMP”), iminodisuccinic acid (“IDA”), N-(2-sulfomethyl)-aspartic acid (“SMAS”), N-(2-sulfoethyl)-aspartic acid (“SEAS”), N-(2-sulfomethyl)- glutamic acid (“SMGL”), N-(2-sulfoethyl)-glutamic acid (“SEGL”), N-methyliminodiacetic acid (“MIDA”), 15 α-alanine-N,N-diacetic acid (“α-ALDA”), serine-N,N-diacetic acid (“SEDA”), isoserine-N,N-diacetic acid (“ISDA”), phenylalanine-N,N-diacetic acid (“PHDA”), anthranilic acid-N,N-diacetic acid (“ANDA”), sulfanilic acid-N,N-diacetic acid (“SLDA”), taurine-N,N-diacetic acid (“TUDA”) and sulfomethyl- N,N-diacetic acid (“SMDA”), N-(2-hydroxyethyl)-ethylidenediamine-N,N’,N’-triacetate (“HEDTA”), diethanolglycine (“DEG”), diethylenetriamine penta(methylenephosphonic acid) (“DTPMP”), 20 aminotris(methylenephosphonic acid) (“ATMP”), and combinations and salts thereof. Preferred builder BZcomprised in the cleaning formulation F according to the instant invention are selected from the group of aminopolycarboxylates, like N,N-dicarboxymethyl glutamic acid and methylglycine N,N-diacetic acid, citrates, polyaspartic acids and polyglutamic acids and their salts. 25 I.5.1.4 Solvents In a preferred embodiment, cleaning formulation F may comprise at least one solvent selected from water or non-aqueous solvent. It is preferred that cleaning formulation F comprises water, and that it is an aqueous mixture. Such aqueous mixture optionally contains at least one non-aqueous solvent. 30 In those embodiments where cleaning formulation F is an aqueous mixture, it is preferred that the content of water in cleaning formulation F is from 1 wt.-% to 99 wt.-%, more preferably from 10 wt.-% to 99 wt.-%, more preferably from 30 wt.-% to 98 wt.-%, more preferably from 50 wt.-% to 97 wt.-%, more preferably from 60 wt.-% to 96 wt.-%, more preferably from 70 wt.-% to 95 wt.-%, more preferably from 80 wt.-% to 90 wt.-%, wherein the weight-% give the percentage of water relative to the total weight of the mixture. 35 Where cleaning formulation F comprises at least one non-aqueous solvent (preferably in addition to water), suitable non-aqueous solvents include monohydric or polyhydric alcohols, alkanolamines or glycol ethers, provided they are miscible with water in the specified concentration range. The solvents are preferably selected from ethanol, n-propanol, iso-propanol, butanols, glycol, propanediol, butanediol, 40 glycerine, diglycol, propyldiglycol, butyldiglycol, hexylene glycol, ethylene glycol methyl ether, ethylene202400143 Foreign Filings 35 glycol ethyl ether, ethylene glycol propyl ether, n-butyl glycol ether, ethylene glycol mono-glycol ether, diethylene glycol ethyl ether, propylene glycol methyl ether, propylene glycol ethyl ether, propylene glycol propyl ether, dipropylene glycol monomethyl ether, dipropylene glycol monoethyl ether, diisopropylene glycol monomethyl ether, diisopropylene glycol monoethyl ether, methoxy triglycol, ethoxy triglycol, 5 butoxy triglycol, 1-butoxyethoxy-2-propanol, n-butoxyethoxy-2-propanol, di-butoxyethoxy-2-propanol, 3-butyl-3-methoxyether solvents, and mixtures of these solvents, butoxyethoxy-2-propanol, 3-butyl-3-butyl ether, propyl glycol, di-octanol ether, di-butoxy-2-propanol, propylenglycol, di-butoxyethoxy-2- propanol, di-butoxyethoxy-2-propanol, 3-butoxy-3-methoxyether solvents, diisopropylene glycol monomethylether, diisopropylene glycol monomethylether, and mixtures of these solvents. Cleaning formulation F preferably10 contains a polyol as the non-aqueous solvent. The polyol can comprise glycerol, 1,2-propanediol, 1,3- propanediol, ethylene glycol, diethylene glycol and / or dipropylene glycol. In those embodiments where cleaning formulation F comprises at least one non-aqueous solvent, the amount of all non-aqueous solvents in cleaning formulation F is preferably between 0.5 wt.-% to 15 wt.-%, 15 preferably 1 wt.-% to 10 wt.-%, relative to the total weight of cleaning formulation F. I.5.1.5 Preservatives In a preferred embodiment, cleaning formulation F may comprise at least one preservative. Exemplary preservatives include ascorbic acid, phenoxyethanol, sodium levulinate, sodium benzoate, p-anisic acid, 20 potassium sorbate, benzoic acid, glyceryl caprylate, capryl glycol, pentylene glycol, methyl propane diol, bronopol, isothiazolinone (methylisothiazolinone, chloromethylisothiazolinone). In those embodiments where cleaning formulation F comprises at least one preservative, the amount of all preservatives in cleaning formulation F is preferably between 0.001 wt.-% to 2 wt.-%, preferably 25 0.01 wt.-% to 0.1 wt.-%, relative to the total weight of cleaning formulation F. I.5.1.6 Benefit agent In a preferred embodiment, cleaning formulation F comprises at least one benefit agent. A benefit agent is preferably provided in an encapsulate. The cleaning formulation F may also comprise an unconfined 30 (also called non-encapsulated) benefit agent, for example a volatile benefit agent. Where the volatile benefit agent is a perfume, the perfumes are suitable for use as the encapsulated volatile benefit agent and also as the unconfined perfume component. Preferred encapsulates in this context comprise shear / pressure-sensitive action encapsulates, whereby 35 the sensorial benefit agent is released in response to mechanical force (e.g. friction, pressure, shear stress) on the encapsulate. The encapsulate shell is preferably comprised of materials including but not limited to polyurethane, polyamide, polyolefine, polysaccharide, protein, silicone, lipid, modified cellulose, gums, polyacrylate, polyphosphate, polystyrene, polyesters or combinations of these materials.202400143 Foreign Filings 36 Preferably, the benefit agent is selected from the group consisting of a sensorial benefit agent, a skin benefit agent, an olfactory benefit agent, more preferably a sensorial benefit agent. The most preferred benefit agent is a perfume. The benefit agent may be a volatile benefit agent. 5 Sensorial benefit agents may also have benefits for hair and / or hard surfaces and / or fabrics. The sensorial benefit may have anti-foam properties, and as such it is advantageous for foaming purposes that it is encapsulated so as not to inter with the foam until release by rubbing. Suitable volatile benefit agents include but are not limited to perfumes, insect repellents, essential oils, sensates such as menthol and aromatherapy actives, preferably perfumes. Mixtures of volatile benefit agents may be used. 10 In those embodiments where cleaning formulation F comprises at least one benefit agent, the total amount of benefit agent is preferably from 0.01 wt.-% to 10 wt.-%, more preferably from 0.05 wt.-% to 5 wt.-%, even more preferably from 0.1 wt.-% to 4.0 wt.-%, most preferably from 0.15 wt.-% to 4.0 wt.-%, based on the total weight of the cleaning formulation F. I.5.1.7 Polymers 15 In a preferred embodiment, cleaning formulation F comprises at least one polymer for use in detergents that are different from the polymers described before. The polymer may function as a co-builder as mentioned above, or may provide a further anti-redeposition effect or one function selected from fiber protection, soil release, dye transfer inhibition, viscosity modifiers, grease cleaning and / or anti-foaming 20 properties. Exemplary polymers include (carboxymethyl)cellulose (“CMC”), poly(vinyl alcohol) (“PVA”), poly(vinylpyrrolidone) (“PVP”), poly(ethyleneglycol) or poly(ethylene oxide) (“PEG”), ethoxylated poly(ethyleneimine), carboxymethyl inulin (“CMI”), and polycarboxylates such as PAA, PAA / PMA, poly- aspartic acid, and lauryl methacrylate / acrylic acid copolymers, hydrophobically modified CMC (“HM-CMC”) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of 25 poly(ethylene terephthalate) and poly(oxyethylene terephthalate) (“PET-POET”), PVP, poly(vinylimidazole) (“PVI”), poly(vinylpyridine-N-oxide) (“PVPO” or “PVPNO”) and polyvinylpyrrolidone- vinylimidazole (“PVPVI”). Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (“PEO-PPO”) and diquaternium ethoxy sulfate. Other exemplary polymers are disclosed in, e.g., WO 2006 / 130575 A2. Salts of the above-mentioned polymers are also 30 contemplated. Preferably a cleaning formulation F according to the instant invention is characterized in that it comprises at least one selected from anti-redeposition polymers and soil release polymers, with soil release polymers being preferred. This has the technical effect, that the cleaning capabilities of the cleaning 35 formulation F according to the instant invention is even more enhanced. It is preferred in the context of the instant invention, that the anti-redeposition polymer or soil release polymer is selected from the group consisting of modified cellulose, preferably carboxymethylcellulose, cellulose acetate and methylcellulose, modified starch, modified inulin, preferably carboxy methyl inulin, polyitaconic acid, polyvinylpyrrolidone, polyvinyl alcohol, and polyethylene glycol, with carboxymethylcellulose and methylcellulose being most 40 preferred.202400143 Foreign Filings 37 Further preferred soil release polymers are water soluble polyesters as for example from the TexCare® range commercially available under the name TexCare SRN 260, TexCare SRN 170, TexCare SRN 260 Life and combinations thereof, as well as the soil release polymers disclosed in WO 2016 / 075178 A1, 5 WO 2016 / 075179 A1, EP 3489340 A1, and EP 3489338 A1. Further preferred soil release polymers are selected from carboxy methyl inulins. A commercial example is Carboxyline®CMI. EP 1746109 A2 discloses hybrid polymers of amylose and acrylates, that can also advantageously be used in the cleaning formulation F of the instant invention as soil release polymers. A commercial example for this type of soil release polymers is Alcoguard® H 5941. 10 Non-limiting examples of biopolymers include: starch, like e.g. corn starch, Zea mays starch and tapioca starch, modified starch, like e.g. starch hydroxypropyltrimonium chloride and hydrolyzed corn starch, cellulose, bacterial cellulose, modified cellulose, like e.g. microcrystalline cellulose, hydroxypropyl methylcellulose and cetyl hydroxyethylcellulose, guar gum, pectin, inulin, carrageenan, alginate, galactoarabinan, polycitronellol, carboxymethyl inulin, carboxymethyl cellulose, polyitaconic acid and 15 combinations and salts thereof. In those embodiments where cleaning formulation F comprises at least one polymer, the amount of all polymers in cleaning formulation F is preferably from 0.05 wt.-% to 8 wt.-%, preferably from 0.1 wt.-% to 5 wt.-%, relative to the total weight of cleaning formulation F. 20 I.5.1.8 Other Additives In a preferred embodiment, cleaning formulation F comprises at least one further additives selected from the group consisting of bleaching systems, anti-redeposition aids, fibre protection agents, soil release agents, dye transfer inhibitors, fabric hueing agents, blueing dyes, enzyme stabilizing agents like boric 25 acid, pH-regulators, emollients, emulsifiers, thickeners / viscosity regulators / stabilizers, UV photoprotective filters, antioxidants, hydrotropes (or polyols), solids and fillers, film formers, pearlescent additives, deodorant and antiperspirant active ingredients, insect repellents, self-tanning agents, preservatives, conditioners, perfumes, dyes, odour absorbers, cosmetic active ingredients, care additives, superfatting agents, solvents, malodor removers. 30 Substances which can be used as exemplary representatives of the individual groups are known to the person skilled in the art and can be found for example in US 2011 / 0091399 A1. I.5.2 Form of the cleaning formulation F The form of the cleaning formulation F depends on the area of use. 35 In particular in those cases, where the cleaning formulation F is used for cleaning an object O, in particular in cases where the object O is a woven or non-woven article A or where object O is crockery (e.g. dishes, cups) or cutlery, the cleaning formulation F may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a 40 regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid. There202400143 Foreign Filings 38 are a number of detergent formulation forms such as layers (same or different phases), pouches, as well as forms for machine dosing unit. Pouches can be configured as single or multi-compartments. They can be of any form, shape and material which is suitable for holding the cleaning formulation F, e.g. without allowing the release of the 5 cleaning formulation F from the pouch prior to water contact. The pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch. Preferred films are polymeric materials, preferably polymers which are formed into a film or sheet. Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, 10 hydroxyethyl cellulose, hydroxypropyl methyl cellulose, maltodextrin, poly methacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (“HPMC”). Preferably the level of polymer in the film, for example PVA, is at least about 60 wt.-%. The preferred average molecular weight of the polymer will typically be from about 20,000 g / mol to about 150,000 g / mol. Films can also be of blend compositions comprising hydrolytically degradable and water soluble polymer blends such as 15 polyactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by Chris Craft In. Prod. Of Gary, Ind., US) plus plasticizers like glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof. The pouches can comprise a solid laundry detergent composition or part components and / or a liquid cleaning composition or part components separated by the water-soluble film. The compartment for liquid components can be different in composition than compartments containing solids, see for example 20 US 2009 / 0011970 A1. Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets. Thereby negative storage interaction between components can be avoided. Different dissolution profiles of each of the compartments can also give rise to delayed dissolution of selected components in the wash solution. 25 In those cases where the cleaning formulation F is a detergent composition for body, i.e. in which the cleaning formulation F is used to clean the human or animal body B, according to the instant invention, the cleaning formulation F can be in form of a laundry soap bar and used for hand washing laundry, fabrics and / or textiles. The “term laundry soap bar” includes laundry bars, soap bars, combo bars, syndet 30 bars and detergent bars. The types of bar usually differ in the type of surfactant they contain, and the term laundry soap bar includes those containing soaps from fatty acids and / or synthetic soaps. The laundry soap bar has a physical form which is solid and not a liquid, gel or a powder at room temperature. The term “solid” is defined as a physical form which does not significantly change over time, i.e. if a solid object (e.g. laundry soap bar) is placed inside a container, the solid object does not change to fill the 35 container it is placed in. The bar is a solid typically in bar form but can be in other solid shapes such as round or oval. Cleaning formulation F, in particular in those embodiments where it is a detergent composition for household care, can be formulated as a granular detergent as described in WO 2009 / 092699 A1, EP 1705241 A1, EP 1382668 A1, WO 2007 / 001262 A1, US 6,472,364 B1, WO 2004 / 074419 A2, or 40 WO 2009 / 102854 A1.202400143 Foreign Filings 39 Nevertheless, in those cases where the cleaning formulation F is a detergent composition for body, i.e. in which the cleaning formulation F is used for cleaning the human or animal body B, according to the instant invention, the cleaning formulation F preferably is in the form of a liquid or gel detergent. This may be aqueous, typically containing at least 20 wt.-% water, with the percentages referring to the total weight 5 of cleaning formulation F. Other types of liquids, including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel. Where cleaning formulation F is an aqueous liquid or gel detergent, it preferably contains from 0 wt-% to 30 wt.-% organic solvent, more preferably 1 wt.-% to 25 wt.-%, even more preferably 5 wt.-% to 15 wt.-%, with the percentages referring to the total weight of cleaning formulation F. While a liquid or gel detergent may be non-aqueous, it is 10 preferred that such liquid or gel detergent comprises water. Where the cleaning formulation F is a detergent composition for body, it is characterized in that the pH of such composition at 25 °C is from 3.0 to 9.0, preferably from 4.0 to 7.0 and particularly preferably from 5.0 to 6.6. 15 I.5.3 Further Bacillus / Priestia strains in the cleaning formulation F The cleaning formulation F according to the present invention may, in particular in addition to Priestia megaterium DSM 34980 and mutants thereof, comprise further strains with advantageous cleaning properties, preferably at least one strain selected from Bacillus velezensis DSM 34674 and mutants 20 thereof (described under item II.), Bacillus licheniformis DSM 34977 and mutants thereof (described under item III.), Bacillus velezensis DSM 34978 and mutants thereof (described under item IV.), Bacillus subtilis DSM 34981 and mutants thereof (described under item V.). The cleaning formulation F according to the present invention may further comprising at least one of the 25 following: - Bacillus velezensis DSM 34674 and / or mutants thereof; - Bacillus licheniformis DSM 34977 and / or mutants thereof; - Bacillus velezensis DSM 34978 and / or mutants thereof; - Bacillus subtilis DSM 34981 and / or mutants thereof. 30 I.6 Use of the cleaning formulation F for cleaning an object O or the human or animal body B In a further aspect, the present invention relates to the use of the cleaning formulation F for cleaning an object O or the human or animal body B. In case where the human or animal body B is cleaned, such use is cosmetic only and hence non-therapeutic. 35 In those embodiments where the cleaning formulation F is used for cleaning the human or animal body B according to the invention, this means that the cleaning formulation F is applied to a living human being or animal. In the embodiment wherein B is selected from skin, hair, is cleaned, this means that the respective part of B of the living human animal is cleaned. 40202400143 Foreign Filings 40 The use according to the present invention is for cleaning. In those embodiments where the cleaning formulation F is used for cleaning the human or animal body B according to the invention, the use is hence cosmetic, and non-therapeutic. It goes without saying that in those preferred embodiments where the object O is cleaned, the method is also non-therapeutic, since the object O is lifeless. 5 In case the cleaning formulation F is used for cleaning the human or animal body B, it is preferred that the cleaning formulation F is used for cleaning at least a part of the human or animal body selected from skin, hair, most preferred hair. 10 An “object O” is a lifeless object and preferably comprises at least one material selected from natural fibre, ceramic, metal, plastic, glass, stone and may also be a liquid such as an aqueous solution. In case the cleaning formulation F is used for cleaning an object O, the object O in a preferred embodiment is selected from the group consisting of a woven, a non-woven, a vehicle, crockery, cutlery, 15 food storage containers, furniture, flooring, panelling, paving, domestic machine, garden tool, construction equipment, building for livestock or domestic animal, music instrument, toy, window. The object O, in particular, is selected from the group consisting of a woven, a non-woven, furniture, flooring, panelling, even more preferably selected from the group consisting of a woven, a non-woven. I.7 Method of cleaning an object O or the human or animal body B 20 In a further aspect, the present invention relates to a method of cleaning an object O or the human or animal body B comprising the following steps: (a) contacting O or B with an, optionally diluted, cleaning formulation F according to the invention, 25 wherein the Priestia megaterium DSM 34980 or a mutant thereof comprised by F is caused to produce protease activity before or while, preferably while, the, optionally diluted, cleaning formulation F is in contact with O or B, (b) separating at least a part of F from O or B, (c) optionally rinsing O or B with further water. 30 The method according to the invention is hence a method of cleaning an object O or the human or animal body B. In those embodiments where the human or animal body B is cleaned in the method according to the 35 invention, it is preferred that at least a part of the human or animal body selected from skin, hair, most preferred hair, is cleaned. An “object O” is a lifeless object and preferably comprises at least one material selected from natural fibre, ceramic, metal, plastic, glass, stone, and may also be a liquid such as an aqueous solution. 40202400143 Foreign Filings 41 An “aqueous solution is, in particular, selected from sewage water, manure and slurry. “Natural fibre” in the context of the invention preferably is one selected from the group consisting of vegetable fibres, animal fibres. Typical vegetable fibres are based on cellulose and in particular selected 5 from wood, cotton, hemp, jute, flax, abaca, piña (pineapple fibre), ramie, sisal, bagasse, banana. Preferably, vegetable fibres are selected from the group consisting of wood, cotton. Vegetable fibres may for example be found in paper, cardboard. Typical animal fibres are in particular selected from the group consisting of wool, silk. 10 The object O in a preferred embodiment is selected from the group consisting of a woven, a non-woven, a vehicle, crockery, cutlery, food storage containers, furniture, flooring, panelling, paving, domestic machine, garden tool, construction equipment, building for livestock or domestic animal, music instrument, toy, window. The object O, in particular, is selected from the group consisting of a woven, a 15 non-woven, furniture, flooring, panelling, even more preferably selected from the group consisting of a woven, a non-woven. The woven is in particular selected from an article of clothing, curtains, napkins, bed linen, tablecloth, blanket, bedspread, duvet cover. 20 The non-woven is in particular selected from an article of clothing, curtains, napkins, bed linen, tablecloth, blanket, bedspread, duvet cover. The article of clothing is in particular selected from the group consisting of sweaters, shirts, pants, shoes, 25 socks, hosiery, coats, haberdashery, suits, hats, caps, bonnets, scarfs, gloves. The vehicle is in particular selected from the group consisting of car, train (which may be selected from the group consisting of railroad cars, tram cars, underground railway cars), plane, bicycle, motor-bike, rocket, water vehicles (which may be selected from ships, boats, hovercraft). 30 Crockery is in particular selected from the group consisting of dishes, glassware (such as drinking glasses), cups, platters, mugs, pitchers, pots, cannikins. Cutlery is in particular selected from the group consisting of knives, forks, spoons, chopsticks. 35 Food storage containers are in particular selected from the group consisting of barrels, lunchboxes, bottles, jars. Furniture is in particular selected from the group consisting of shelves, boards, wardrobes, cupboards, 40 desks, tables, chairs, chest of drawers.202400143 Foreign Filings 42 Flooring is in particular selected from the group consisting of laminate floor, parquet floor, tiled floor, carpeted floor, ceramic floor. Panelling is in particular selected from the group consisting of wallpaper, wall tiles, tapestry. 5 Paving may be any kind of road surface, and is in particular selected from cobblestone, asphalt, gravel. A domestic machine may be any electric machine used in the household, and is in particular selected from washing machine, dishwasher, vacuum cleaner, sound system, lamp, TV, computer, printer, heater, 10 electrical kitchen appliances such as fridge, oven, stove, boiler, egg boiler, toaster, sandwich maker, waffle iron, mixer, bread machine, yogurt maker, coffee maker, electric kettle. A garden tool is preferably selected from the group consisting of rake, grate, lawnmower, scythe, spade, shovel. 15 Construction equipment is in particular any equipment, electrical or non-electrical, which may be used in handcraft or in construction of buildings, roads. Construction equipment is preferably selected from drilling machines, tools such as hammer, rasp, screwdriver. 20 Building for livestock or domestic animal is in particular any container or building in which pets or farm animals may be kept. In particular, the building for livestock or domestic animal is selected from the group consisting of terrarium, aquarium, cage, pen, kennel, cowshed, hennery, pigsty, coop. Music instrument may be any keyboard instrument, string instrument, wind instrument, percussion 25 instrument and is preferably selected from piano, guitar, drums. Toy is preferably selected from video game console, doll. Window may be any transparent light opening, and is particular selected from outside window of a 30 building, inside window of a building, bull’s eyes of washing machines, bull’s eyes of ships, preferably selected from outside window of a building, inside window of a building. In those embodiments where the human or animal body B is cleaned in the method according to the invention, this means that the method according to the invention is applied to a living human being or 35 animal. In the embodiment wherein B is selected from skin, hair, is cleaned, this means that the respective part of B of the living human being or animal is cleaned. The method according to the present invention is a method of cleaning. In those embodiments where the human or animal body B is cleaned in the method according to the invention, the method is hence a 40 cosmetic method, and non-therapeutic. It goes without saying that in those preferred embodiments where the object O is cleaned, the method is also non-therapeutic, since the object O is lifeless.202400143 Foreign Filings 43 I.7.1 Step (a) In step (a) of the method of the invention, the object O or the human or animal body B is contacted with 5 the cleaning formulation F according to the invention, wherein the Priestia megaterium strain DSM 34980 or a mutant comprised by F is caused to produce protease activity before or while F is in contact with O or B. Optionally, the cleaning formulation F applied in step (a) of the method according to the invention is 10 diluted. In those embodiments where the cleaning formulation F is diluted, it is preferred that such dilution is carried out with water. The optional dilution may take place before or while F is in contact with O and B. Preferably, the optional dilution takes place while F is in contact with O and B. The optional dilution of the cleaning formulation F with water W may be carried out according the skilled 15 person’s knowledge and depends on the context in which the method according to the invention is carried out. For example, in those embodiments where object O is cleaned, and O is selected from woven, non- woven, crockery, cutlery, and the method is for example carried out in a washing machine or dishwasher, 20 respectively, the water for dilution may simply be provided through the water tap to which the respective machine is connected. Likewise, in those embodiments where the human or animal body B is cleaned, and in particular a part of the body selected from skin and hair is cleaned, the water for dilution may simply be provided through the 25 water tap to which the respective tap (e.g. shower head) is connected. For example, in case the method according to the invention is carried out in a device which is selected from a dishwasher, in those embodiments where the object O is crockery or cutlery, or a washing machine, in those embodiments where the object O is woven or non-woven, the cleaning formulation F is 30 provided in the detergent compartment, while water is provided during the wash. The cleaning formulation F and water are then mixed, for example in the wash drum of the washing machine. In step (a) of the method according to the invention, object O or the human or animal body B is contacted with the optionally diluted cleaning formulation F. 35 “Contacting the object O / the human or animal body B with F” is a further essential feature of the method according to the invention. This is to be understood as meaning that F and at least a part of the surface of the object O / the human or animal body B are in direct contact. In the context of the present invention “in direct contact” is to be understood as meaning “wetting” of the 40 object O / the human or animal body B with F. It will be appreciated that the object O / the human or202400143 Foreign Filings 44 animal body B and the cleaning formulation F are thus in direct contact at a contact surface of object O / the human or animal body B. The method according to the invention is a cleaning method. The gist of the method according to the 5 present invention lies in the fact that the Priestia megaterium strain DSM 34980 or a mutant thereof comprised by F is caused to produce protease activity before or while, preferably while, F is in contact with O or B. This means in particular that during step (a), at least one impurity I which is absorbed or adsorbed on the object O or the human or animal body B is at least partially desorbed and thus removed from the object O 10 or the human or animal body B and dispersed or dissolved, in particular dispersed, in the, optionally diluted, cleaning formulation F. In other words: in step (a), the, optionally diluted, cleaning formulation F is brought in direct contact with at least a part of the surface of object O or the human or animal body B, onto which at least one impurity I is absorbed or adsorbed, so that the at least one impurity I is at least partially desorbed or degraded and thus removed from the object O or the human or animal body B. The 15 optionally degraded impurity I is then dispersed or dissolved, in particular dispersed, in the, optionally diluted, cleaning formulation F. Therefore, in particular, after step (a), an optionally diluted cleaning formulation F is obtained wherein at least one impurity I in dissolved or dispersed, preferably dispersed. The impurity I may either be in the form of a liquid (e.g. droplet) or a particle, and preferably is a particle. 20 In a preferred embodiment, the impurity I is at least one impurity which may be inorganic or organic, and is preferably organic. Organic impurities are preferably selected from oils and fats, which may be of vegetable, animal or synthetic origin, food based particles, soil, pollen, sebum, body fluids, for example, blood, sperm, sweat, urine, feces, liquor. 25 Inorganic impurities are preferably selected from the group consisting of carbon black, fine dust, plastic particles (e.g. microplastic particles), metal oxides (preferably iron oxide), silica (such as sand), clay, dyes (such as pigments), more preferably clay, in particular kaolin. Since the gist of the invention lies in the outstanding activity of Priestia megaterium strain DSM 34980 or a mutant thereof to produce protease activity, it is preferred that at least a part of the impurities I cleaned 30 during the method of the invention are the substrates of these activities. Hence, it is preferred that the impurity I which is cleaned from the object O or the human or animal body B during the cleaning method according to the invention is selected from the group consisting of proteins (in particular proteins selected from casein and whey protein), in particular proteins selected from casein and whey protein. 35 Furthermore, in step (a), the Priestia megaterium DSM 34980 or a mutant thereof comprised by F is caused to produce protease activity before or while F is in contact with O or B. Hence, it is preferred that,202400143 Foreign Filings 45 in step (a), the Priestia megaterium DSM 34980 or a mutant thereof comprised by F is caused to produce at least protease activity while F is in contact with O or B. The skilled person may adjust the conditions at which the Priestia megaterium strain DSM 34980 or a 5 mutant thereof produces protease activity. Typically, the activity is triggered when the Priestia megaterium strain DSM 34980 or a mutant thereof during step (a) are contacted with the respective impurity, in particular proteins (which triggers the protease activity). In addition, in step (a) of the method according to the invention, Priestia megaterium strain DSM 34980 or 10 the mutant of Priestia megaterium strain DSM 34980 may also be contacted with at least one from the group consisting of nutrients, salts. Preferred nutrients are selected from carbohydrates, amino acids, peptides. 15 Peptides are preferably selected from peptone. As amino acid, any of the natural amino acids may be selected by the skilled person. Preferably, the amino acid is selected from the group consisting of glutamine, alanine, valine, aspartate, glutamate, methionine, asparagine, preferably alanine, valine, asparagine. Carbohydrates are preferably sugars, polysaccharides. 20 Preferred sugars are glucose, saccharose, fructose, galactose. Preferred polysaccharides are starch, inulin. Preferred salts are salts selected from sodium chloride, potassium phosphate, di-potassium hydrogen phosphate. 25 Priestia megaterium strain DSM 34980 or the mutant of Priestia megaterium strain DSM 34980 may also be contacted in step (a) of the method according to the invention with further additives known to the skilled person such as tris(hydroxymethyl)aminomethane (“Tris”). 30 It is hence preferred, that, if the object O is cleaned in the method according to the invention, the temperature in step (a) is in a range of from 10 °C to < 100 °C, in particular of from 20 °C to 95 °C, preferably of from 25 °C to 65 °C, more preferably of from 30 °C to 45 °C. If the human or animal body B is cleaned in the method according to the invention, and preferably in 35 those embodiments where skin or hair, is cleaned, it is preferred that the temperature in step (a) is in a range of from 15 °C to 45 °C, in particular of from 20 °C to 40 °C, preferably of from 25 °C to 35 °C. In a further preferred embodiment, the contacting step (a) is carried out for at least 1 second (“second” = “s”), preferably at least 10 s, preferably for at least 1 minute (“minute” = “min”), more preferably for at least 40 5 min, preferably for at least 15 min, more preferably from 15 min to 240 min, more preferably from 30 min to 180 min, more preferably from 45 min to 120 min.202400143 Foreign Filings 46 Preferably, in those cases where F is diluted with water in step (a), it is preferred that the pH of the water in F in step (a) at 25 °C is from 3.5 to 9, preferably from 5 to 9, preferably from 6 to 9, and particularly preferably from 7 to 8. 5 In a particular embodiment of step (a) of the method according to the invention, the Priestia megaterium strain DSM 34980 or a mutant thereof comprised by the optionally diluted cleaning formulation F contacts valeric acid, preferably valeric acid in dissolved form in an aqueous solution LVal, wherein the concentration (weight-%) of valeric acid in LValis more preferably ≤ 5000 ppm, in particular in the range of 10 from 1 ppt to 5000 ppm, more preferably in the range of from 1 ppb to 3000 ppm, even more preferably in the range of from 10 ppb to 2000 ppm, even more preferably in the range of from 20 ppb to 1000 ppm, even more preferably in the range of from 30 ppb to 1000 ppm, even more preferably in the range of from 50 ppb to 1000 ppm, even more preferably in the range of from 100 ppb to 1000 ppm, even more preferably in the range of from 1 ppm to 1000 ppm, even more preferably in the range of from 10 ppm to 15 1000 ppm, even more preferably in the range of from 100 ppm to 1000 ppm, relative to the total weight of LVA. Preferably, the Priestia megaterium strain DSM 34980 or mutant thereof comprised by the optionally diluted cleaning formulation F is then also caused to metabolize valeric acid. Priestia megaterium strain DSM 34980 or mutant thereof comprised by the optionally diluted cleaning formulation F is caused to metabolize valeric acid under the same conditions under which they produce at least one of protease, 20 cellulase, amylase activity. The aqueous solution LValcomprising valeric acid may be any liquid film containing valeric acid that usually forms as soon as water as part of cleaning formulation F contacts the respective surface for example during the performance of step (a) of the method of the invention. In case of the human or 25 animal body B, such aqueous solution LValmay also be selected from sweat, blood, sperm, urine, feces. In case of an object O, such aqueous solution LValmay also form from rain or condensed water from the air humidity that condensates on the object O and mixes with valeric acid which was absorbed on object O. 30 This embodiment is, in addition, advantageous, as valeric acid is a typical source of malodor, and Priestia megaterium strain DSM 34980 and mutants thereof are able to metabolize valeric acid, as shown under item IV.2 of the example section. I.7.2 Step (b) 35 In step (b) of the method of the invention, at least a part of F is separated from O or B. The separation is, in a preferred embodiment, carried out so that F is essentially complete separated from object O or the animal or body part B.202400143 Foreign Filings 47 The skilled person is aware of how to carry out this separation in each specific context. Generally, this separation is carried out by withdrawing the object O or the animal or body part B from at least a part of the optionally diluted F. 5 An object O subjected to step (b), is optionally subjected to centrifugation (for example in a washing machine). I.7.3 Optional step (c) 10 In an optional step (c) of the method according to the invention, the object O or the animal or body part B is rinsed with further water. This water employed in optional step (c) is preferably from the same source as water provided in step (a). I.8 Feed or Food E and method of feeding animals 15 Due to their enzymatic activities the microorganisms and microbial preparations of the invention, i.e. Priestia megaterium DSM 34980 and mutants thereof, are also useful as food or feed additive for foods and feeds, in particular to help in the digestion and utilization of other food and feed ingredients. The present invention thus also refers to a food or feed E comprising at least one of Priestia megaterium 20 DSM 34980 strain and a mutant of Priestia megaterium DSM 34980 strain according to the invention or a preparation thereof according to the invention. Hence, the present invention, in a further aspect, also relates to a a food or feed E comprising at least one of Priestia megaterium DSM 34980, a mutant of Priestia megaterium DSM 34980, a preparation of 25 Priestia megaterium DSM 34980, a preparation of a mutant of Priestia megaterium DSM 34980. Preparations are described above (paragraph I.4). It is preferred that the a food or feed E comprises at least one of Priestia megaterium DSM 34980 strain and mutants of Priestia megaterium DSM 34980 strain. It is further preferred that the a food or feed E comprises cells of Priestia megaterium DSM 34980 strain 30 and / or mutants thereof in a living state. In a preferred embodiment, the food or feed E comprises the Priestia megaterium DSM 34980 and / or a mutant thereof or the preparation thereof in a carrier-bound form. 35 The carrier is preferably selected from anti-caking agents, antioxidants, bulking agents, binders, structurants, coatings and / or protectants. Examples of useful carriers include polysaccharides (in particular starches, maltodextrins, celluloses, methylcelluloses, gums like guar gum, xanthan gum and gum arabic, wheat middlings, corn cob meal, chitosan and / or inulins), protein sources (in particular skim milk powder, sweet-whey powder, gelatine and / or soy flour), protein hydrolysates (in particular gelatine, 40 yeast extract and / or peptones like soy peptone), peptides, sugars (in particular lactose, trehalose,202400143 Foreign Filings 48 sucrose, dextrose and / or maltose), lipids (in particular lecithin, vegetable oils and / or mineral oils), salts (in particular sodium chloride, sodium carbonate, calcium carbonate, chalk, limestone, magnesium carbonate, sodium phosphate, calcium phosphate, magnesium phosphate and / or sodium citrate), silicates (in particular clays, zeolites, Fuller’s earth, clinoptilolite, montmorillonite, perlite, vermiculite, 5 diatomaceous earth, talc, bentonites, kaolin clay, silica in particular precipitated silica, hydrophobic silica and / or hydrophilic silica, and / or silicate salts like aluminium, magnesium and / or calcium silicate), silica gel, silica dioxide, activated carbon, lignite, magnesium and calcium oxide. The foods and feeds of the invention preferably comprise at least one further food or feed additive, in 10 particular selected from the carriers as mentioned above, proteins, carbohydrates, fats, feed concentrates, silage, mashfeed, probiotics, prebiotics, enzymes, vitamins, immune modulators, milk replacers, minerals, amino acids, carriers, in particular as mentioned above, coccidiostats, acid-based products and / or medicines, in particular antibiotics. 15 A further subject of the invention is therefore also a method of feeding animals, wherein the animals are fed with feed or food E, in particular for facilitating the digestion of other feed ingredients. A further subject of the invention is therefore also the use of feed or food E for feeding animals, in particular for facilitating the digestion of other feed ingredients. 20 The method according to the invention of feeding animals is non-therapeutic. The animals are, in particular, selected from livestock, cattle (in particular cow), poultry (in particular chicken, ostrich, quail, goose, duck), fish (which may be farmed fish, such as salmon, trout, or catfish of 25 the genus Pangasius, or ornamental fish such as fish of the genus Pterophyllum such as Pterophyllum scalare, of the genus Chromobotia such as Chromobotia macracanthus, of the genus Trichogaster such as Trichogaster leeri), sheep, goat, pig. The feed or food E according to the present invention may, in particular in addition to Priestia megaterium 30 DSM 34980 and mutants thereof, comprise further strains with advantageous cleaning properties, preferably at least one strain selected from Bacillus velezensis DSM 34674 and mutants thereof (described under item II.), Bacillus licheniformis DSM 34977 and mutants thereof (described under item III.), Bacillus velezensis DSM 34978 and mutants thereof (described under item IV.), Bacillus subtilis DSM 34981 and mutants thereof (described under item V.). 35 The feed or food E according to the present invention may further comprising at least one of the following: - Bacillus velezensis DSM 34674 and / or mutants thereof; - Bacillus licheniformis DSM 34977 and / or mutants thereof; - Bacillus velezensis DSM 34978 and / or mutants thereof; 40 - Bacillus subtilis DSM 34981 and / or mutants thereof.202400143 Foreign Filings 49 II. Bacillus velezensis strain DSM 34674 and mutants In a further aspect, the present invention relates to the Bacillus velezensis strain as deposited under DSM 34674 at the DSMZ and mutants thereof. B. velezensis DSM 34674 and / or mutants thereof may be 5 comprised by the cleaning formulation F or food or feed E, preferably by the cleaning formulation F. “Bacillus velezensis DSM 34674” relates to the Bacillus velezensis strain as deposited under DSM 34674 at the DSMZ (abbreviated as “B. velezensis DSM 34674” or “Bacillus velezensis DSM 34674” or simply “DSM 34674”). 10 It was surprisingly found that Bacillus velezensis DSM 34674 and mutants thereof exhibit a high expression of enzymatic activity for protease and cellulase, and also have good enzymatic activity for amylase (confer point I. of the Examples) and therefore are particularly well suited to be used in cleaning formulations and in animal feeding, preferably in cleaning formulations. 15 In addition, it was surprisingly found that Bacillus velezensis DSM 34674 and mutants thereof exhibit a high rate of metabolization of valeric acid (1000 ppm), as set forth under point IV. of the Examples. The mutants of Bacillus velezensis DSM 34674 are also Bacillus velezensis strains and may be obtained 20 by any kind of method, i.e., by genetic modification methods (“GMO”) or non-GMO methods, but preferably the mutants of Bacillus velezensis DSM 34674 are not genetically modified, i.e., non-GMO. It goes without saying that a mutant of Bacillus velezensis DSM 34674 is not identical with Bacillus velezensis DSM 34674. This means that the mutants of the deposited strain of Bacillus velezensis DSM 34674 are preferably either also naturally occurring microorganisms or spontaneous mutants of such 25 naturally occurring microorganisms, i.e. of the deposited strains, or microorganisms which are obtained by another method which is classified as non-GMO. Preferred mutants of Bacillus velezensis DSM 34674 display property (β), even more preferably display properties (α) and (β) as described under point II.2. 30 It is even more preferred that, alternatively or in addition, preferably in addition, the mutants of Bacillus velezensis DSM 34674 have at least characteristic (2) as follows, wherein it is even more preferred that they have at least characteristics (1) and (2) as follows: (1) a DNA sequence identity (in particular of the genomic DNA of the mutant) to the genomic DNA sequence of B. velezensis DSM 34674 as set forth under point II.1.1); 35 (2) at least one, preferably at least two, more preferably at least three, even more preferably at least four, even more preferably at least five, most preferably all six characteristics i., ii., iii., iv., v. and vi. as set forth under point II.1.2). II.1 Mutants of Bacillus velezensis DSM 34674 defined by DNA sequence identity 40202400143 Foreign Filings 50 II.1.1) Sequence identity to genomic DNA In a preferred embodiment of the present invention, the term “mutant of DSM 34674” refers to Bacillus velezensis strains with a DNA sequence identity (in particular of the genomic DNA of the mutant) of at 5 least 95 %, more preferred of at least 97 %, more preferred of at least 98 %, more preferred of at least 99 %, more preferred of at least 99.5 %, more preferred of at least 99.8 %, more preferred of at least 99.9 %, more preferred of at least 99.95 %, more preferred of at least 99.98 %, more preferred of at least 99.99 %, more preferred of at least 99.999 %, more preferred of at least 99.9999 % to the genomic DNA sequence of Bacillus velezensis DSM 34674. 10 The “genomic sequence of Bacillus velezensis DSM 34674” is available / can be determined from the deposited strain Bacillus velezensis DSM 34674 by means according to the state of the art (for example, as summarized in the reviews by T. Hu, N. Chitnis, D. Monos, A. Dinh, Human Immunology 2021, 82, 801-811; S. Levy & E. Boone, Cold Spring Harbor Perspectives in Medicine 2019, 9, a025791). 15 II.1.2) Sequence identity to conserved DNA sequences The following sequences are typical, conserved sequences of Bacillus velezensis DSM 34674: 1. SEQ ID NO: 1: a DNA sequence coding for the 16S rRNA sequence; 20 2. SEQ ID NO: 2: a rpoB sequence; 3. SEQ ID NO: 3: a gyrB sequence; 4. SEQ ID NO: 4: a groEL sequence; 5. SEQ ID NO: 5: a yqfD sequence; 6. SEQ ID NO: 6: a uvrC sequence. 25 In a further preferred embodiment, the mutant of DSM 34674 exhibits at least one, preferably at least two, more preferably at least three, even more preferably at least four, even more preferably at least five, most preferably all six of the following characteristics: i. a DNA sequence, which preferably is the DNA sequence coding for the 16S rRNA, with a 30 sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 1; and / or ii. a DNA sequence, which preferably is a rpoB DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more 35 preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 2; and / or iii. a DNA sequence, which preferably is a gyrB DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 3; and / or202400143 Foreign Filings 51 iv. a DNA sequence, which preferably is a groEL DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 4; and / or v. a DNA sequence, which preferably is a yqfD DNA sequence, with a sequence identity of 5 at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 5; and / or vi. a DNA sequence, which preferably is a uvrC DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 6. 10 In a most preferred embodiment, the mutant of DSM 34674 exhibits all six characteristics i., ii., iii., iv., v. and vi. 15 “A DNA sequence with a certain sequence identity, in particular with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 1, 2, 3, 4, 5, or 6” means those DNA sequences that display the respective sequence identity when such sequence identity is determined by comparison of the DNA sequence over its whole length to SEQ ID NO: 1, 2, 3, 4, 5, or 6, respectively, over the whole length 20 of SEQ ID NO: 1, 2, 3, 4, 5, or 6, respectively. II.2 Mutants of Bacillus velezensis DSM 34674 defined by function Bacillus velezensis DSM 34674 has high protease activity and cellulase activity, as summarized under 25 point I.4 of the Example section. In particular, the protease activity of Bacillus velezensis DSM 34674 is surprisingly superior to prior art Bacillus velezensis strains. Preferably, protease activity in case of Bacillus velezensis DSM 34674 and mutants thereof means protease activity in the supernatant, i.e. secreted protease activity, as determined by the test according to Assay A-I. Preferably, cellulase activity in case of Bacillus velezensis DSM 34674 and mutants thereof means cellulase activity as determined by 30 the test according to Assay C. Bacillus velezensis DSM 34674 according to the invention has excellent amylase activities. Preferably, amylase activity in case of B. velezensis DSM 34674 and mutants thereof means amylase activities as determined by the test according to Assay E. In addition, Bacillus velezensis DSM 34674 according to the invention has improved activities in terms of 35 metabolization of valeric acid (1000 ppm). In the context of the method according to the first aspect of the invention and the use according to the second aspect of the invention, those mutants of Bacillus velezensis DSM 34674 are preferred that display property (β), even more preferably display properties (α) and (β) as follows: 40202400143 Foreign Filings 52 (α) the mutant of Bacillus velezensis DSM 34674 is able to metabolize valeric acid (1000 ppm), even more preferably is able to metabolize valeric acid (5000 ppm), wherein, even more preferably, the ability to metabolize valeric acid VA (1000 ppm) as well as the ability to metabolize valeric acid VA (5000 ppm) is determined by the test according to Assay J; 5 (β) the mutant of Bacillus velezensis DSM 34674 has protease activity (wherein, even more preferably, the protease activity is determined by the test according to Assay A-I), where it is more preferred that the mutant of Bacillus velezensis DSM 34674 has protease activity (wherein, even more preferably, the protease activity is determined by the test according to Assay A-I) 10 and cellulase activity (wherein, even more preferably, the cellulase activity is determined by the test according to Assay C), wherein it is even more preferred that the mutant of Bacillus velezensis DSM 34674 has protease activity (wherein, even more preferably, the protease activity is determined by the test according to Assay A-I), cellulase activity (wherein, even more preferably, the cellulase activity is determined by the test according 15 to Assay C), and amylase activity (wherein, even more preferably, the amylase activity is determined by the test according to Assay E). II.2.1) Mutant of Bacillus velezensis DSM 34674 with ability to metabolize VA Where a mutant of Bacillus velezensis DSM 34674 (= “Mutant 34674”) is able to metabolize valeric acid 20 VA at a given concentration xVA of VA, wherein in particular xVA = 1000 ppm and preferably xVA = 5000 ppm, it is preferred that, for this concentration xVA, the metabolization rate kXJ%(xVA) of valeric acid VA exhibited by the Mutant 34674 relative to the metabolization rate of valeric acid VA of Bacillus velezensis DSM 34674 is at least 50 %, preferably at least 60 %, preferably at least 65 %, preferably at least 70 %, preferably at least 75 %, preferably at least 85 %, preferably at least 86 %, preferably at least 87 %, 25 preferably at least 88 %, preferably at least 89 %, preferably at least 90 %, more preferably at least 91 %, more preferably at least 92 %, more preferably at least 93 %, more preferably at least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at least 97 %, more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.6 %, more preferably at least 99.7 %, more preferably at least 99.8 %, more preferably at least 99.9 %, more preferably at least 30 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 %, wherein kXJ% (xVA) is, in particular, determined by the test according to Assay L-II (point VI.5.3.2). II.2.2) Mutant of Bacillus velezensis DSM 34674 with protease activity 35 Where a mutant of Bacillus velezensis DSM 34674 has protease activity, it is further preferred that the mutant of Bacillus velezensis DSM 34674 has a protease activity which is at least 85 %, preferably at least 86 %, preferably at least 87 %, preferably at least 88 %, preferably at least 89 %, preferably at least 90 %, more preferably at least 91 %, more preferably at least 92 %, more preferably at least 93 %, more 40 preferably at least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at202400143 Foreign Filings 53 least 97 %, more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 % the protease activity of Bacillus velezensis DSM 34674, wherein the protease 5 activity of the mutant of Bacillus velezensis DSM 34674 relative to the protease activity of Bacillus velezensis DSM 34674 is, in particular, determined by the test according to Assay B-II (point VI.1.2). II.2.3) Mutant of Bacillus velezensis DSM 34674 with cellulase activity Where a mutant of Bacillus velezensis DSM 34674 has cellulase activity, it is further preferred that the 10 mutant of Bacillus velezensis DSM 34674 has a cellulase activity which is at least 60 %, preferably at least 65 %, preferably at least 70 %, preferably at least 75 %, preferably at least 85 %, preferably at least 86 %, preferably at least 87 %, preferably at least 88 %, preferably at least 89 %, preferably at least 90 %, more preferably at least 91 %, more preferably at least 92 %, more preferably at least 93 %, more preferably at least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at 15 least 97 %, more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.6 %, more preferably at least 99.7 %, more preferably at least 99.8 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 % the cellulase activity of Bacillus velezensis DSM 34674, wherein the cellulase 20 activity of the mutant of Bacillus velezensis DSM 34674 relative to the cellulase activity of Bacillus velezensis DSM 34674 is, in particular, determined by the test according to Assay D-II (point VI.2.2). II.2.4) Mutant of Bacillus velezensis DSM 34674 with amylase activity Where a mutant of Bacillus velezensis DSM 34674 has amylase activity, it is further preferred that the 25 mutant of Bacillus velezensis DSM 34674 has an amylase activity which is at least 99 %, more preferably at least 99.5 %, more preferably at least 99.6 %, more preferably at least 99.7 %, more preferably at least 99.8 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 % the amylase activity of Bacillus 30 velezensis DSM 34674, wherein the amylase activity of the mutant of Bacillus velezensis DSM 34674 relative to the amylase activity of Bacillus velezensis DSM 34674 is, in particular, determined by the test according to Assay F-II (point VI.3.2). 35 III. Bacillus licheniformis strain DSM 34977 and mutants In a further aspect, the present invention relates to the Bacillus licheniformis strain as deposited under DSM 34977 at the DSMZ and mutants thereof. B. licheniformis DSM 34977 and / or mutants thereof may be comprised by the cleaning formulation F or food or feed E, preferably by the cleaning formulation F.202400143 Foreign Filings 54 “Bacillus licheniformis DSM 34977” relates to the Bacillus licheniformis DSM 34977 strain as deposited under DSM 34977 at the DSMZ (abbreviated as “B. licheniformis DSM 34977” or “Bacillus licheniformis DSM 34977” or simply “DSM 34977”). 5 It was surprisingly found that B. licheniformis DSM 34977 and mutants thereof exhibit a high ability to grow on valeric acid (1000 ppm) and exhibit a high rate of metabolization of valeric acid (1000 ppm), as set forth under point IV. of the Examples, and therefore are particularly well suited to be used in cleaning formulations and in animal feeding, preferably in cleaning formulations. 10 Therefore, they are particularly well suited to be used in cleaning formulations F, in particular in those embodiments of the method according to the invention, in which in step (a), the optionally diluted cleaning formulation F contacts valeric acid, preferably valeric acid in dissolved form in an aqueous solution LVal. This is yet another reason why they are particularly well suited to be used in cleaning formulations. 15 The mutants of B. licheniformis DSM 34977 are also Bacillus licheniformis strains and may be obtained by any kind of method, i.e., by genetic modification methods (“GMO”) or non-GMO methods, but preferably the mutants of Bacillus licheniformis DSM 34977 are not genetically modified, i.e., non-GMO. It goes without saying that a mutant of B. licheniformis DSM 34977 is not identical with B. licheniformis 20 DSM 34977. This means that the mutants of the deposited strain of B. licheniformis DSM 34977 are preferably either also naturally occurring microorganisms or spontaneous mutants of such naturally occurring microorganisms, i.e. of the deposited strains, or microorganisms which are obtained by another method which is classified as non-GMO. 25 Preferred mutants of Bacillus licheniformis DSM 34977 display property (γ), even more preferably display properties (γ) and (δ) as described under point III.2. It is even more preferred that, alternatively or in addition, preferably in addition, the mutants of Bacillus licheniformis DSM 34977 have at least characteristic (2) as follows, wherein it is even more preferred that they have at least characteristics (1) and (2) as follows: 30 (1) a DNA sequence identity (in particular of the genomic DNA of the mutant) to the genomic DNA sequence of Bacillus licheniformis DSM 34977 as set forth under point III.1.1); (2) at least one, preferably at least two, more preferably at least three, even more preferably at least four, even more preferably at least five, most preferably all six characteristics i., ii., iii., iv., v. and vi. as set forth under point III.1.2). 35 III.1 Mutants of B. licheniformis DSM 34977 definedIII.1.1) Sequence identity to genomic DNA In a preferred embodiment of the present invention, the term “mutant of DSM 34977” refers to Bacillus 40 licheniformis strains with a DNA sequence identity (in particular of the genomic DNA of the mutant) of at202400143 Foreign Filings 55 least 95 %, more preferred of at least 97 %, more preferred of at least 98 %, more preferred of at least 99 %, more preferred of at least 99.5 %, more preferred of at least 99.8 %, more preferred of at least 99.9 %, more preferred of at least 99.95 %, more preferred of at least 99.98 %, more preferred of at least 99.99 %, more preferred of at least 99.999 %, more preferred of at least 99.9999 % to the genomic DNA 5 sequence of B. licheniformis DSM 34977. The “genomic sequence of B. licheniformis DSM 34977” is available / can be determined from the deposited strain B. licheniformis DSM 34977 by means according to the state of the art (for example, as summarized in the reviews by T. Hu, N. Chitnis, D. Monos, A. Dinh, Human Immunology 2021, 82, 801- 10 811; S. Levy & E. Boone, Cold Spring Harbor Perspectives in Medicine 2019, 9, a025791). III.1.2) Sequence identity to conserved DNA sequences The following sequences are typical, conserved sequences of B. licheniformis DSM 34977: 15 - SEQ ID NO: 19: a DNA sequence coding for the 16S rRNA sequence; - SEQ ID NO: 20: a rpoB sequence; - SEQ ID NO: 21: a gyrB sequence; - SEQ ID NO: 22: a groEL sequence; - SEQ ID NO: 23: a yqfD sequence; 20 - SEQ ID NO: 24: an adaA sequence. In a further preferred embodiment, the mutant of DSM 34977 exhibits at least one, preferably at least two, more preferably at least three, even more preferably at least four, even more preferably at least five, most preferably all six of the following characteristics i. to vi.: 25 i. a DNA sequence, which preferably is the DNA sequence coding for the 16S rRNA, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 19; and / or ii. a DNA sequence, which preferably is a rpoB DNA sequence, with a sequence identity of 30 at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 20; and / or iii. a DNA sequence, which preferably is a gyrB DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 21; and / or 35 iv. a DNA sequence, which preferably is a groEL DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 22; and / or v. a DNA sequence, which preferably is a yqfD DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more 40 preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 23; and / or202400143 Foreign Filings 56 vi. a DNA sequence, which preferably is an adaA DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 24. 5 In a most preferred embodiment, the mutant of B. licheniformis DSM 34977 exhibits all six characteristics i., ii., iii., iv., v., and vi. “A DNA sequence with a certain sequence identity, in particular with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the 10 polynucleotide sequence according to SEQ ID NO: 19, 20, 21, 22, 23, or 24” means those DNA sequences that display the respective sequence identity when such sequence identity is determined by comparison of the DNA sequence over its whole length to SEQ ID NO: 19, 20, 21, 22, 23, or 24, respectively, over the whole length of SEQ ID NO: 19, 20, 21, 22, 23, or 24, respectively. 15 III.2 Mutants of B. licheniformis DSM 34977 defined by function Bacillus licheniformis DSM 34977 according to the invention has improved activities in terms of growth on 1000 ppm valeric acid and metabolization of valeric acid, as shown under point IV. of the Example section. Preferably, the ability to grow on valeric acid (1000 ppm) and the metabolization of valeric acid in 20 case of Bacillus licheniformis DSM 34977 and mutants thereof is determined by the test according to Assay J (point VII.5.1). In the context of the method according to the first aspect of the invention and the use according to the second aspect of the invention, those mutants of Bacillus licheniformis DSM 34977 are preferred that 25 display property (γ), more preferably display properties (γ) and (δ) as follows: (γ) the mutant of Bacillus licheniformis DSM 34977 is able to grow on valeric acid (1000 ppm), even more preferably is able to grow on valeric acid (5000 ppm), wherein, even more preferably, the ability to grow on VA (1000 ppm) as well as the ability to grow on VA (5000 ppm) is determined by the test according to 30 Assay J, wherein “able to grow on valeric acid (1000 ppm)” means in particular that they fulfill the condition “ΓXJ;1000 ppm > 1” for xVA = 1000 ppm as determined by the test according to Assay J (point VI.5.1.4.1) and wherein “able to grow on valeric acid (5000 ppm)” means in particular that they fulfill the condition “ΓXJ;5000 ppm> 1 for xVA= 5000 ppm as determined by the test according to Assay J (point VI.5.1.4.2); 35 (δ) the mutant of Bacillus licheniformis DSM 34977 has an effectiveness ΕXJ% (xVA) to reduce valeric acid [wherein xVA= 1000 ppm, preferably xVA= 5000 ppm] which is at least 85 %, preferably at least 86 %, preferably at least 87 %, preferably at least 88 %, preferably at least 89 %, preferably at least 90 %, more preferably at least 91 %, more preferably at least 92 %, more preferably at least 93 %, more preferably at 40 least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at least 97 %,202400143 Foreign Filings 57 more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 % relative to the effectiveness of Bacillus licheniformis DSM 34977 to reduce 5 valeric acid, wherein ΕXJ%(xVA) [wherein xVA= 1000 ppm, preferably xVA= 5000 ppm] is, in particular, determined by the test according to Assay K-I (point VI.5.2.1). IV. Bacillus velezensis strain DSM 34978 and mutants In a further aspect, the present invention relates to the Bacillus velezensis strain as deposited under 10 DSM 34978 at the DSMZ and mutants thereof. B. velezensis DSM 34978 and / or mutants thereof may be comprised by the cleaning formulation F or food or feed E, preferably by the cleaning formulation F. “Bacillus velezensis DSM 34978” relates to the Bacillus velezensis strain as deposited under DSM 34978 at the DSMZ (abbreviated as “B. velezensis DSM 34978” or “Bacillus velezensis DSM 34978” or simply 15 “DSM 34978”). It was surprisingly found that Bacillus velezensis DSM 34978 and mutants thereof exhibit a high expression of enzymatic activity for protease, amylase, and cellulase (confer point I. of the Examples), and therefore are particularly well suited to be used in cleaning formulations and in animal feeding, 20 preferably in cleaning formulations. In addition, it was surprisingly found that Bacillus velezensis DSM 34978 and mutants thereof exhibit a high rate of metabolization of valeric acid (1000 ppm), as set forth under point IV. of the Examples. 25 The mutants of Bacillus velezensis DSM 34978 are also Bacillus velezensis strains and may be obtained by any kind of method, i.e., by genetic modification methods (“GMO”) or non-GMO methods, but preferably the mutants of Bacillus velezensis DSM 34978 are not genetically modified, i.e., non-GMO. It goes without saying that a mutant of Bacillus velezensis DSM 34978 is not identical with B. velezensis DSM 34978. This means that the mutants of the deposited strain of B. velezensis DSM 34978 are 30 preferably either also naturally occurring microorganisms or spontaneous mutants of such naturally occurring microorganisms, i.e. of the deposited strains, or microorganisms which are obtained by another method which is classified as non-GMO. Preferred mutants of B. velezensis DSM 34978 display property (β), even more preferably display 35 properties (α) and (β) as described under point IV.2. It is even more preferred that, alternatively or in addition, preferably in addition, the mutants of Bacillus velezensis DSM 34978 have at least characteristic (2) as follows, wherein it is even more preferred that they have at least characteristics (1) and (2) as follows: (1) a DNA sequence identity (in particular of the genomic DNA of the mutant) to the genomic DNA 40 sequence of B. velezensis DSM 34978 as set forth under point IV.1.1);202400143 Foreign Filings 58 (2) at least one, preferably at least two, more preferably at least three, even more preferably at least four, even more preferably at least five, most preferably all six characteristics i., ii., iii., iv., v. and vi. as set forth under point IV.1.2). 5 IV.1 Mutants of B. velezensis DSM 34978 definedIV.1.1) Sequence identity to genomic DNA In a preferred embodiment of the present invention, the term “mutant of DSM 34978” refers to Bacillus 10 velezensis strains with a DNA sequence identity (in particular of the genomic DNA of the mutant) of at least 95 %, more preferred of at least 97 %, more preferred of at least 98 %, more preferred of at least 99 %, more preferred of at least 99.5 %, more preferred of at least 99.8 %, more preferred of at least 99.9 %, more preferred of at least 99.95 %, more preferred of at least 99.98 %, more preferred of at least 99.99 %, more preferred of at least 99.999 %, more preferred of at least 99.9999 % to the genomic DNA 15 sequence of B. velezensis DSM 34978. The “genomic sequence of B. velezensis DSM 34978” is available / can be determined from the deposited strain B. velezensis DSM 34978 by means according to the state of the art (for example, as summarized in the reviews by T. Hu, N. Chitnis, D. Monos, A. Dinh, Human Immunology 2021, 82, 801-811; S. Levy & 20 E. Boone, Cold Spring Harbor Perspectives in Medicine 2019, 9, a025791). IV.1.2) Sequence identity to conserved DNA sequences The following sequences are typical, conserved sequences of Bacillus velezensis DSM 34978; - SEQ ID NO: 7: a DNA sequence coding for the 16S rRNA sequence; 25 - SEQ ID NO: 8: a rpoB DNA sequence; - SEQ ID NO: 9: a gyrB DNA sequence; - SEQ ID NO: 10: a groEL DNA sequence; - SEQ ID NO: 11: a DNA sequence coding for an ATP synthase C chain; - SEQ ID NO: 12: a DNA sequence coding for a chemotaxis protein sequence. 30 In a further preferred embodiment, the mutant of Bacillus velezensis DSM 34978 exhibits at least one, preferably at least two, more preferably at least three, even more preferably at least four, even more preferably at least five, most preferably all six of the following characteristics i. to vi.: i. a DNA sequence, which preferably is the DNA sequence coding for a 16S rRNA, with a 35 sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 7;202400143 Foreign Filings 59 ii. a DNA sequence, which preferably is a rpoB DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 8; iii. a DNA sequence, which preferably is a gyrB DNA sequence, with a sequence identity of 5 at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 9; iv. a DNA sequence, which preferably is a groEL DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 10; 10 v. a DNA sequence, which preferably is a DNA sequence coding for an ATP synthase C chain, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 11; vi. a DNA sequence, which preferably is a DNA sequence coding for a chemotaxis protein, 15 with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 12. In a most preferred embodiment, the mutant of B. velezensis DSM 34978 exhibits all six characteristics i., 20 ii., iii., iv., v., and vi. “A DNA sequence with a certain sequence identity, in particular with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the 25 polynucleotide sequence according to SEQ ID NO: 7, 8, 9, 10, 11, or 12” means those DNA sequences that display the respective sequence identity when such sequence identity is determined by comparison of the DNA sequence over its whole length to SEQ ID NO: 7, 8, 9, 10, 11, or 12, respectively, over the whole l of SEQ ID NO: 7, 8, 9, 10, 11, or 12, respectively. 30 IV.2 Mutants of B. velezensis DSM 34978 defined by function Bacillus velezensis DSM 34978 has high activities in terms of protease activity, amylase activity, cellulase activity, as summarized under point I.4 of the Example section. In particular, the protease activity of Bacillus velezensis DSM 34978 is surprisingly superior to prior art Bacillus velezensis strains. Preferably, 35 protease activity in case of Bacillus velezensis DSM 34978 and mutants thereof means protease activity in the supernatant, i.e. secreted protease activity, as determined by the test according to Assay A-I. Preferably, cellulase activity in case of Bacillus velezensis DSM 34978 and mutants thereof means cellulase activity as determined by the test according to Assay C. Preferably, amylase activity in case of B. velezensis DSM 34978 and mutants thereof means amylase activity as determined by the test 40 according to Assay E.202400143 Foreign Filings 60 In addition, B. velezensis DSM 34978 according to the invention has improved activities in terms of metabolization of valeric acid (1000 ppm). 5 In the context of the invention, those mutants of Bacillus velezensis DSM 34978 are preferred that display property (β), even more preferably display properties (α) and (β) as follows: (α) the mutant of Bacillus velezensis DSM 34978 is able to metabolize valeric acid (1000 ppm), even more preferably is able to metabolize valeric acid (5000 ppm), wherein, even more preferably, the ability 10 to metabolize valeric acid VA (1000 ppm) as well as the ability to metabolize valeric acid VA (5000 ppm) is determined by the test according to Assay J; (β) the mutant of Bacillus velezensis DSM 34978 has protease activity (wherein, even more preferably, the protease activity is determined by the test according to Assay A-I), 15 wherein it is more preferred that the mutant of Bacillus velezensis DSM 34978 has protease activity (wherein, even more preferably, the protease activity is determined by the test according to Assay A-I) and cellulase activity (wherein, even more preferably, the cellulase activity is determined by the test according to Assay C), 20 where it is even more preferred that the mutant of Bacillus velezensis DSM 34978 has protease activity (wherein, even more preferably, the protease activity is determined by the test according to Assay A-I), cellulase activity (wherein, even more preferably, the cellulase activity is determined by the test according to Assay C), and amylase activity (wherein, even more preferably, the amylase activity is determined by the test according to Assay E). 25 IV.2.1) Mutant of Bacillus velezensis DSM 34978 with ability to metabolize VA Where a mutant of Bacillus velezensis DSM 34978 (= “Mutant 34978”) is able to metabolize valeric acid VA at a given concentration xVAof valeric acid (= “VA”), wherein in particular xVA= 1000 ppm and 30 preferably xVA= 5000 ppm, it is preferred that, for this concentration xVA, the metabolization rate kXJ%(xVA) of valeric acid exhibited by the Mutant 34978 relative to the metabolization of valeric acid of Bacillus velezensis DSM 34978 is at least 50 %, at least 60 %, preferably at least 65 %, preferably at least 70 %, preferably at least 75 %, preferably at least 85 %, preferably at least 86 %, preferably at least 87 %, preferably at least 88 %, preferably at least 89 %, preferably at least 90 %, more preferably at least 91 %, 35 more preferably at least 92 %, more preferably at least 93 %, more preferably at least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at least 97 %, more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.6 %, more preferably at least 99.7 %, more preferably at least 99.8 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101202400143 Foreign Filings 61 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 %, wherein kXJ%(xVA) is, in particular, determined by the test according to Assay L-I (point VI.5.3.1). IV.2.2) Mutant of Bacillus velezensis DSM 34978 with protease activity 5 Where a mutant of Bacillus velezensis DSM 34978 has protease activity, it is further preferred that such mutant of Bacillus velezensis DSM 34978 has a protease activity which is at least 85 %, preferably at least 86 %, preferably at least 87 %, preferably at least 88 %, preferably at least 89 %, preferably at least 90 %, more preferably at least 91 %, more preferably at least 92 %, more preferably at least 93 %, more preferably at least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at 10 least 97 %, more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 % the protease activity of Bacillus velezensis DSM 34978, wherein the protease activity of the mutant of Bacillus velezensis DSM 34978 relative to the protease activity of Bacillus 15 velezensis DSM 34978 is, in particular, determined by the test according to Assay B-I (point VI.1.2) IV.2.3) Mutant of Bacillus velezensis DSM 34978 with cellulase activity Where a mutant of Bacillus velezensis DSM 34978 has cellulase activity, it is further preferred that such mutant of Bacillus velezensis DSM 34978 has a cellulase activity which is at least 60 %, preferably at 20 least 65 %, preferably at least 70 %, preferably at least 75 %, preferably at least 85 %, preferably at least 86 %, preferably at least 87 %, preferably at least 88 %, preferably at least 89 %, preferably at least 90 %, more preferably at least 91 %, more preferably at least 92 %, more preferably at least 93 %, more preferably at least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at least 97 %, more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.6 %, 25 more preferably at least 99.7 %, more preferably at least 99.8 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 % the cellulase activity of Bacillus velezensis DSM 34978, wherein the cellulase activity of the mutant of Bacillus velezensis DSM 34978 relative to the cellulase activity of Bacillus 30 velezensis DSM 34978 is, in particular, determined by the test according to Assay D-I (point VI.2.2). IV.2.4) Mutant of Bacillus velezensis DSM 34978 with amylase activity Where a mutant of B. velezensis DSM 34978 has amylase activity, it is further preferred that such mutant of Bacillus velezensis DSM 34978 has an amylase activity which is at least 99 %, more preferably at least 35 99.5 %, more preferably at least 99.6 %, more preferably at least 99.7 %, more preferably at least 99.8 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 % the amylase activity of Bacillus velezensis DSM 34978, wherein the amylase activity of the mutant of Bacillus velezensis DSM 34978 relative to the202400143 Foreign Filings 62 amylase activity of Bacillus velezensis DSM 34978 is, in particular, determined by the test according to Assay F-I (point VI.3.2). V. Bacillus subtilis strain DSM 34981 and mutants 5 In a further aspect, the present invention relates to the Bacillus subtilis strain as deposited under DSM 34981 at the DSMZ and mutants thereof. B. subtilis DSM 34981 and / or mutants thereof may be comprised by the cleaning formulation F or food or feed E, preferably by the cleaning formulation F. “Bacillus subtilis DSM 34981” relates to the Bacillus subtilis DSM 34981 strain as deposited under 10 DSM 34981 at the DSMZ (abbreviated as “B. subtilis DSM 34981” or “Bacillus subtilis DSM 34981” or simply “DSM 34981”). It was surprisingly found that Bacillus subtilis DSM 34981 and mutants thereof exhibit a high expression of enzymatic activity for lipase (confer point III. of the Examples) and therefore are particularly well suited 15 to be used in cleaning formulations and in animal feeding, preferably in cleaning formulations. In addition, it was surprisingly found that Bacillus subtilis DSM 34981 and mutants thereof exhibit a high ability to grow on valeric acid (1000 ppm) and exhibit a high rate of metabolization of valeric acid (1000 ppm), as set forth under point IV. of the Examples. 20 The mutants of B. subtilis DSM 34981 are also Bacillus subtilis strains and may be obtained by any kind of method, i.e., by genetic modification methods (“GMO”) or non-GMO methods, but preferably the mutants of Bacillus subtilis DSM 34981 are not genetically modified, i.e., non-GMO. It goes without saying that a mutant of B. subtilis DSM 34981 is not identical with B. subtilis DSM 34981. This means that the 25 mutants of the deposited strain of B. subtilis DSM 34981 are preferably either also naturally occurring microorganisms or spontaneous mutants of such naturally occurring microorganisms, i.e. of the deposited strains, or microorganisms which are obtained by another method which is classified as non-GMO. Preferred mutants of Bacillus subtilis DSM 34981 display property (ζ), more preferably display properties 30 (γ) and (ζ), even more preferably display properties (γ), (δ), and (ζ) as described under point V.2. It is even more preferred that, alternatively or in addition, preferably in addition, the mutants of Bacillus subtilis DSM 34981 have at least characteristic (2) as follows, wherein it is even more preferred that they have at least characteristics (1) and (2) as follows: (1) a DNA sequence identity (in particular of the genomic DNA of the mutant) to the genomic DNA 35 sequence of Bacillus subtilis DSM 34981 as set forth under point V.1.1); (2) at least one, preferably at least two, more preferably at least three, even more preferably at least four, even more preferably at least five, most preferably all six characteristics i., ii., iii., iv., v. and vi. as set forth under point V.1.2).202400143 Foreign Filings 63 V.1 Mutants of B. subtilis DSM 34981 defined by DNA sequence identity V.1.1) Sequence identity to genomic DNA 5 In a preferred embodiment of the present invention, the term “mutant of DSM 34981” refers to Bacillus subtilis strains with a DNA sequence identity (in particular of the genomic DNA of the mutant) of at least 95 %, more preferred of at least 97 %, more preferred of at least 98 %, more preferred of at least 99 %, more preferred of at least 99.5 %, more preferred of at least 99.8 %, more preferred of at least 99.9 %, more preferred of at least 99.95 %, more preferred of at least 99.98 %, more preferred of at least 10 99.99 %, more preferred of at least 99.999 %, more preferred of at least 99.9999 % to the genomic DNA sequence of B. subtilis DSM 34981. The “genomic sequence of B. subtilis DSM 34981” is available / can be determined from the deposited strain B. subtilis DSM 34981 by means according to the state of the art (for example, as summarized in 15 the reviews by T. Hu, N. Chitnis, D. Monos, A. Dinh, Human Immunology 2021, 82, 801-811; S. Levy & E. Boone, Cold Spring Harbor Perspectives in Medicine 2019, 9, a025791). V.1.2) Sequence identity to conserved DNA sequences The following sequences are typical, conserved sequences of B. subtilis DSM 34981: 20 1. SEQ ID NO: 13: a DNA sequence coding for the 16S rRNA sequence; 2. SEQ ID NO: 14: a rpoB sequence; 3. SEQ ID NO: 15: a gyrB sequence; 4. SEQ ID NO: 16: a groEL sequence; 25 5. SEQ ID NO: 17: a lipC sequence; 6. SEQ ID NO: 18: a yqcA sequence. In a further preferred embodiment, the mutant of DSM 34981 exhibits at least one, preferably at least two, more preferably at least three, even more preferably at least four, even more preferably at least five, most 30 preferably all six of the following characteristics i. to vi.: i. a DNA sequence, which preferably is the DNA sequence coding for the 16S rRNA, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 13; and / or 35 ii. a DNA sequence, which preferably is a rpoB DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 14; and / or202400143 Foreign Filings 64 iii. a DNA sequence, which preferably is a gyrB DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 15; and / or iv. a DNA sequence, which preferably is a groEL DNA sequence, with a sequence identity of 5 at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 16; and / or v. a DNA sequence, which preferably is a lipC DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 17; and / or 10 vi. a DNA sequence, which preferably is a yqcA DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 18. In a most preferred embodiment, the mutant of B. subtilis DSM 34981 exhibits all six characteristics i., ii., 15 iii., iv., v., and vi. “A DNA sequence with a certain sequence identity, in particular with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 13, 14, 15, 16, 17, or 18” means those DNA 20 sequences that display the respective sequence identity when such sequence identity is determined by comparison of the DNA sequence over its whole length to SEQ ID NO: 13, 14, 15, 16, 17, or 18, respectively, over the whole length of SEQ ID NO: 13, 14, 15, 16, 17, or 18, respectively. V.2 Mutants of B. subtilis DSM 34981 defined by function 25 Bacillus subtilis DSM 34981 has improved activities in terms of lipase activity, as shown under point III. of the Example section. Preferably, lipase activity in case of Bacillus subtilis DSM 34981 and mutants thereof is determined by the test according to Assay G. 30 In addition, Bacillus subtilis DSM 34981 according to the invention has improved activities in terms of growth on 1000 ppm valeric acid and metabolization of valeric acid, as shown under point IV. of the Example section. Preferably, the ability to grow on valeric acid (1000 ppm) and the metabolization of valeric acid in case of Bacillus subtilis DSM 34981 and mutants thereof is determined by the test according to Assay J. 35 In the context of the method according to the first aspect of the invention and the use according to the second aspect of the invention, those mutants of Bacillus subtilis DSM 34981 are preferred that display property (ζ), more preferably display properties (ζ) and (γ), even more preferably display properties (ζ), (γ), and (δ) as follows: 40202400143 Foreign Filings 65 (γ) the mutant of Bacillus subtilis DSM 34981 is able to grow on valeric acid VA (1000 ppm), even more preferably is able to grow on valeric acid VA (5000 ppm), wherein, even more preferably, the ability to grow on VA (1000 ppm) as well as the ability to grow on VA (5000 ppm) is determined by the test according to Assay J, wherein “able to grow on valeric acid (1000 ppm)” means in particular that they 5 fulfill the condition “ΓXJ;1000 ppm> 1” for xVA= 1000 ppm as determined by the test according to Assay J (point VI.5.1.4.1) and wherein “able to grow on valeric acid (5000 ppm)” means in particular that they fulfill the condition “ΓXJ;5000 ppm> 1” for xVA= 5000 ppm as determined by the test according to Assay J (point VI.5.1.4.2); 10 (δ) the mutant of Bacillus subtilis DSM 34981 has an effectiveness ΕXJ%(xVA) to reduce valeric acid VA [wherein xVA= 1000 ppm, preferably xVA= 5000 ppm] which is at least 85 %, preferably at least 86 %, preferably at least 87 %, preferably at least 88 %, preferably at least 89 %, preferably at least 90 %, more preferably at least 91 %, more preferably at least 92 %, more preferably at least 93 %, more preferably at least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at least 97 %, 15 more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 % relative to the effectiveness of Bacillus subtilis DSM 34981 to reduce valeric acid, wherein ΕXJ% (xVA) [wherein xVA = 1000 ppm, preferably xVA = 5000 ppm] is, in particular, 20 determined by the test according to Assay K-III (point VI.5.2.3); (ζ) the mutant of Bacillus subtilis DSM 34981 has lipase activity, it is further preferred that the mutant of Bacillus subtilis DSM 34981 has a lipase activity which is at least 91 %, more preferably at least 92 %, more preferably at least 93 %, more preferably at least 94 %, more preferably at least 95 %, more 25 preferably at least 96 %, more preferably at least 97 %, more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 %, more preferably at least 101 %, more preferably at least 105 %, more preferably at least 110 %, more preferably at least 120 % the lipase activity of B. subtilis DSM 34981, wherein the lipase activity of the mutant of Bacillus subtilis DSM 34981 relative to the lipase 30 activity of Bacillus subtilis DSM 34981 is, in particular, determined by the test according to Assay H (point VI.4.2). VI. Assays for qualification and quantification of catalytic activities and valeric acid metabolism 35 VI.1 Protease activity “Protease activity” in the sense of the present invention is deemed to be an activity that catalyzes the hydrolytic cleavage of a peptide bond linking two amino acid residues (“proteolytic enzymatic activity”). US 2018 / 023040 A1 discloses cleaning compositions comprising proteases, which provide a biocatalytic 40 composition comprising biosurfactants and a protease.202400143 Foreign Filings 66 The prior art describes different assays to qualitatively and quantitatively determine protease activity, for example in Zhang et al., ACS Omega 2021, 6, 3675-3680. 5 In the context of the present invention, two different protease activities may be determined, namely the protease activity that is secreted by a certain strain as well as the total protease activity exerted by a certain strain (i.e. secreted and cell-bound). Assay A-I is the preferred qualitative test for determination of secreted protease activity according to the 10 invention. Assay A-II is the preferred qualitative test for determination of total protease activity according to the invention. 15 Whether a mutant of Bacillus velezensis DSM 34978 exhibits “protease activity” is preferably determined by the test according to Assay A-I further explained in the following. Whether a mutant of Bacillus velezensis DSM 34674 exhibits “protease activity” is preferably determined by the test according to Assay A-I further explained in the following. 20 Whether a mutant of Priestia megaterium DSM 34980 exhibits “protease activity” is preferably determined by the test according to Assay A-II further explained in the following. In order to determine the protease activity (in %) of a given mutant of Bacillus velezensis DSM 34978 25 relative to the protease activity of Bacillus velezensis DSM 34978, the test according to Assay B-I is preferably used. In order to determine the protease activity (in %) of a given mutant of Bacillus velezensis DSM 34674 relative to the protease activity of Bacillus velezensis DSM 34674, the test according to Assay B-II is 30 preferably used. In order to determine the protease activity (in %) of a given mutant of Priestia megaterium DSM 34980 relative to the protease activity of Priestia megaterium DSM 34980, the test according to Assay B-III is preferably used. 35 VI.1.1 Assay A-I Assay A-I may be carried out by the following steps to determine whether a given Strain XAI, for example Bacillus velezensis DSM 34978 or a given mutant of Bacillus velezensis DSM 34978, or Bacillus velezensis DSM 34674 or a given mutant of Bacillus velezensis DSM 34674 exhibit protease activity. 40202400143 Foreign Filings 67 Assay A-I may be used to determine secreted protease activity. (A-I-1) Strain XAIis cultivated in 10 ml tryptic-soy-broth (“TSB”; Merck – 105459; peptone from casein 17.0 g / L; peptone from soymeal 3.0 g / L; D(+) glucose monohydrate 2.5 g / L; sodium chloride 5.0 g / L; 5 di-potassium hydrogen phosphate 2.5 g / L) at 37 °C and 200 rpm for 16 h. As inoculum, 20 µl of a cryo-conservation culture was used for each strain XAI. (A-I-2) After the overnight cultivation, the optical density is measured at λ = 660 nm using a cuvette photometer. A culture volume CM for OD 1 (in 1 ml) is obtained as follows: 10 The culture medium CM is obtained by centrifugation (5000 x g, 3 min, room temperature). The filter- sterile (filtered by 0.2 µm) supernatant is obtained, adjusted (by dilution with TSB medium) to OD 1 and then used (abbreviated as “SNAI”) for the qualitative protease test on specific selective agar plates [step (A-I-3)]. 15 (A-I-3) 10 % Crossley milk agar (“CM0213”, Oxoid; 10 g / L skim milk powder, 1 g / L peptone, 0.01 g / L bromocresol purple, 13 g / L agar-agar) is prepared and 5 µl of the supernatant SNAI [adjusted to OD 1] is dropped on the agar plates. (A-I-4) The agar plates are incubated at 37 °C for 24 h. Through the indicator dye in the agar medium, the 20 elucidation by protease degradation is directly visible. The protease activity is indicated by the extent (area) of the circular / elliptic clearance zone (also referred to as “halo of degradation”). For the determination of the area of the clearance zone, the diameter (in case of a circular clearance zone) or the average value of the largest and smallest diameter (in case of an elliptic circular clearance zone) may be determined. Values are assessed in millimeters (mm) of two independent biological replicates. 25 (A-I-5) As blank control, steps (A-I-1) and (A-I-2) are repeated except that no Strain XAIis cultivated in TSB. In step (A-I-2), the filter-sterile supernatant is diluted in the same ratio as for the tested Strain XAI to give blank culture medium CMAI,Blank. Then, step (A-I-3) is repeated with the difference that 5 µl of CMAI,Blankis dropped on 10 % Crossley milk agar CM0213 prepared as described in step (A-I-3) and 30 incubated for 24 h at 37 °C. (A-I-6) Optionally, as further control and for quantification of the protease activity, the area of a clearance zone may be compared to the area of a clearance zone of a pure protease from Bacillus licheniformis with protease activity of known quantity (typically in the range of from 7-15 U / mg). For this, pure protease 35 from Bacillus licheniformis (subtilisin, P5380, Sigma-Aldrich) is concentrated to 1 mg / ml, and steps (A-I-3) and (A-I-4) are repeated, except that instead of 5 µl of SNAI, 5 µl of the 1 mg / ml solution is used (typically having a calculated activity of around 35-75 µU). By this, the area size of a clearance zone may be correlated to the quantitative value of protease activity. 40 Qualitative assessment of protease activity according to Assay A-I:202400143 Foreign Filings 68 Any Strain XAIthat shows visible protease degradation in step (A-I-4) of Assay A is, in particular, deemed to exhibit the respective protease activity according to the invention. Preferably, any Strain XAthat in step (A-I-4) shows a clearance zone the area of which is larger, preferably at least 10 %, more preferably at least 50 % larger, than the area of the clearance zone observed for CMAI,Blank in step (A-I-5) 5 is deemed to exhibit protease activity. VI.1.2 Assays B-I, B-II Assays B-I and B-II are the preferred quantitative tests for determining the protease activity of a given strain, for example a mutant of Bacillus velezensis DSM 34978 (hereinafter “Mutant 34978”) relative to 10 the protease activity of another given strain, for example Bacillus velezensis DSM 34978; or for example for determining the protease activity of a mutant of Bacillus velezensis DSM 34674 (hereinafter “Mutant 34674”) relative to the protease activity of another given strain, for example Bacillus velezensis DSM 34674. 15 Assay B-I is the preferred quantitative test for determining the protease activity of a mutant of Bacillus velezensis DSM 34978 (hereinafter “Mutant 34978”) relative to the protease activity of Bacillus velezensis DSM 34978. In Assay B-I, the following steps are carried out: 20 (B-I-1) Steps (A-I-1) to (A-I-4) of Assay A-I are carried out, wherein Strain XAI= Bacillus velezensis DSM 34978. The area of the clearance zone obtained at the end of step (A-I-4) is measured and abbreviated as “HBI1”. Step (B-I-1) is repeated three times and the average value of the three measurements of HBI1 is calculated and abbreviated as “ĤBI1”. 25 (B-I-2) Steps (A-I-1) to (A-I-4) of Assay A-I are carried out, wherein Strain XAI= Mutant 34978. The area of the clearance zone obtained at the end of step (A-I-4) is measured and abbreviated as “HBI2”. Step (B-I-2) is repeated three times and the average value of the three measurements of HBI2 is calculated and abbreviated as “ĤBI2”. 30 The percentage of protease activity Aprot exhibited by the Mutant 34978 relative to Bacillus velezensis DSM 34978 is then calculated by Aprot = (ĤBI2 / ĤBI1)*100. Assay B-II is the preferred quantitative test for determining the protease activity of a mutant of Bacillus 35 velezensis DSM 34674 (hereinafter “Mutant 34674”) relative to the protease activity of Bacillus velezensis DSM 34674. In Assay B-II, the following steps are carried out:202400143 Foreign Filings 69 (B-II-1) Steps (A-I-1) to (A-I-4) of Assay A-I are carried out, wherein Strain XAI= Bacillus velezensis DSM 34674. The area of the clearance zone obtained at the end of step (A-I-4) is measured and abbreviated as “HBII1”. Step (B-II-1) is repeated three times and the average value of the three measurements of HBII1 is calculated and abbreviated as “ĤBII1”. 5 (B-II-2) Steps (A-I-1) to (A-I-4) of Assay A-I are carried out, wherein Strain XAI= Mutant 34674. The area of the clearance zone obtained at the end of step (A-I-4) is measured and abbreviated as “HBII2”. Step (B-II-2) is repeated three times and the average value of the three measurements of HBII2 is calculated and abbreviated as “ĤBII2”. 10 The percentage of protease activity AProtexhibited by the Mutant 34674 relative to Bacillus velezensis DSM 34674 is then calculated by AProt = (ĤBII2 / ĤBII1)*100. VI.1.3 Assay A-II 15 Assay A-II may be carried out by the following steps to determine whether a given Strain XAII, for example Priestia megaterium DSM 34980 or a given mutant of Priestia megaterium DSM 34980, exhibits protease activity. 20 Assay A-II may be used to determine total protease activity of an organism (i.e. protease activity that is secreted and cell-bound). (A-II-1) Strain XAII is cultivated on TSA agar medium (“TSA”; peptone from casein 17.0 g / L; peptone from soymeal 3.0 g / L; D(+) glucose monohydrate 2.5 g / L; sodium chloride 5.0 g / L; di-potassium hydrogen 25 phosphate 2.5 g / L) at 37 °C for 16 h. Then the strain XAIIis collected and washed three times with phosphate-buffered saline (“PBS”; Sigma, P4417-100TAB) at 8000 x g centrifugation, 3 min, room temperature, and adjusted by dilution with PBS to an optical density (OD at λ = 600) equal to 0.1. The thus obtained suspension is then used as culture medium CMAII in step (A-II-2). 30 (A-II-2) Skim milk agar medium (skim milk powder 28 g / L, casein enzymatic hydrolysate 5 g / L, yeast extract 2.5 g / L, glucose 1 g / L, agar 15 g / L) is prepared and 10 µl of the respective culture medium CMAII is dropped on the agar plates. (A-II-3) The agar plates are incubated at room temperature for 7 d. The protease activity is indicated by 35 the extent (area) of the circular / elliptic clearance zone (also referred to as “halo of degradation”). For the determination of the area of the clearance zone, the diameter (in case of a circular clearance zone) or the average value of the largest and smallest diameter (in case of an elliptic circular clearance zone) may be determined. Values are assessed in millimeters (mm) of two independent biological replicates.202400143 Foreign Filings 70 (A-II-4) As blank control, step (A-II-2) and step (A-II-3) are repeated except that PBS medium free of any Strain XAIIis cultivated on skim milk agar medium. (A-II-5) Optionally, as further control and for quantification of the protease activity, the area of a clearance 5 zone may be compared to the area of a clearance zone of a pure protease from Bacillus licheniformis with protease activity of known quantity (typically in the range of from 7-15 U / mg). For this, pure protease from Bacillus licheniformis (subtilisin, P5380, Sigma-Aldrich) is concentrated to 1 mg / ml, and steps (A-II-2) and (A-II-3) are repeated, except that instead of 10 µl of CMAII, 5 µl of the 1 mg / ml solution is used (typically having a calculated activity of around 35-75 µU). By this, area size of a clearance zone 10 may be correlated to the quantitative value of protease activity. Qualitative assessment of protease activity according to Assay A-II: Any Strain XAIIthat shows visible protease degradation in step (A-II-3) of Assay A-II is, in particular, 15 deemed to exhibit the respective protease activity according to the invention. Preferably, any Strain XAII that in step (A-II-3) shows a clearance zone the area of which is larger, preferably at least 10 %, more preferably at least 50 % larger, than the area of the clearance zone observed for the blank control in step (A-II-4) is deemed to exhibit protease activity. 20 VI.1.4 Assays B-III Assay B-III is the preferred quantitative test for determining the protease activity of a mutant of Priestia megaterium DSM 34980 (hereinafter “Mutant 34980”) relative to the protease activity of Priestia megaterium DSM 34980. 25 In Assay B-III, the following steps are carried out: (B-III-1) Steps (A-II-1) to (A-II-3) of Assay A-II are carried out, wherein Strain XAII = Priestia megaterium DSM 34980. The area of the clearance zone obtained at the end of step (A-II-3) is measured and 30 abbreviated as “HBIII1”. Step (B-III-1) is repeated three times and the average value of the three measurements of HBIII1 is calculated and abbreviated as “ĤBIII1”. (B-III-2) Steps (A-II-1) to (A-II-3) of Assay A-II are carried out, wherein Strain XAII= Mutant 34980. The area of the clearance zone obtained at the end of step (A-II-3) is measured and abbreviated as “HBIII2”. 35 Step (B-III-2) is repeated three times and the average value of the three measurements of HBIII2 is calculated and abbreviated as “ĤBIII2”. The percentage of protease activity AProtexhibited by the Mutant 34980 relative to Priestia megaterium DSM 34980 is then calculated by AProt = (ĤBII2 / ĤBII1)*100. 40202400143 Foreign Filings 71 VI.2 Cellulase activity: Assay C and Assays D-I,D-II “Cellulase activity” in the sense of the present invention is deemed to be an activity that catalyzes the hydrolytic cleavage of the β-1,4-glykosidic bond of cellulose. 5 The prior art describes different assays to qualitatively and quantitatively determine cellulase activity, for example in Wood & Mahalingeshwara Bhat, Methods in Enzymology 1988, 160, 87-112. Assay C is the preferred qualitative test for cellulase activity according to the invention. 10 Whether a mutant of Bacillus velezensis DSM 34978 or a mutant of Bacillus velezensis DSM 34674 exhibit “cellulase activity” is preferably determined by the following Assay C. In order to determine the cellulase activity (in %) of a given mutant of Bacillus velezensis DSM 34978 15 relative to the cellulase activity of Bacillus velezensis DSM 34978, Assay D-I is preferably used. In order to determine the cellulase activity (in %) of a given mutant of Bacillus velezensis DSM 34674 relative to the cellulase activity of Bacillus velezensis DSM 34674, Assay D-II is preferably used. VI.2.1 Assay C 20 Assay C may be carried out by the following steps to determine whether a given Strain XC, for example Bacillus velezensis DSM 34978 or a given mutant of Bacillus velezensis DSM 34978, or Bacillus velezensis DSM 34674 or a given mutant of Bacillus velezensis DSM 34674, exhibit cellulase activity. 25 (C-1) Strain XCis incubated in a pre-culture in 10 ml VIB medium (Difco Veal Infusion Broth, Ref. 234420) at 37 °C and 200 rpm for 16 h. (C-2) After the incubation, a further culture of 2.5 ml CMC Growth Medium [minimal-salt medium with 10 g / L carboxymethyl cellulose (Sigma 419311)] is inoculated with 125 µl of the pre-culture medium using 30 a small deep-well incubation plate. After inoculation, the further culture is incubated at 37 °C for 24 h at 300 rpm. After 24 h, the OD of the further culture is measured at λ = 660 nm. (C-3) Then, the supernatant SNCof the further culture is harvested by centrifugating of 1 ml aliquot of the further culture in a 1.5 ml Eppendorf tube for 5 min at 13000 rpm. 35 (C-4) 500 µl of the supernatant SNC are subjected to a cellulase activity test using the EnzChek® Cellulase kit from Molecular Probes / Life technologies according to the manufacturer's instructions (E33953). The principle of this test kit is based on the cellulase-catalyzed conversion of the EnzChek® Cellulase Substrate, blue fluorescent, 339 / 452, whereby the fluorescence is enhanced. The detection limit202400143 Foreign Filings 72 is 4 mU / ml to 3 U / ml. To prepare a standard curve for quantification, a 2 U / ml cellulase from Aspergillus niger (Sigma-Aldrich, C1184) and dilutions thereof are prepared. The measurement is performed in black 96-well microtiter plates (Greiner FIA-Plate, black 96K, F-form, 5 655076-225) and in the Tecan plate reader infinite M1000 Pro. Subsequently, the fluorescence is measured at an excitation of λ = 339 nm and an emission of λ = 452 nm. The cellulase activity is calculated based on the standard curve and the activity is normalized to OD 1 (λ = 660 nm) to normalize over cell growth differences after 24 hours incubation at the end of step (C-2). 10 (C-5) As blank control, steps (C-1) to (C-4) are repeated except that the preculture (and logically also the further culture) are cultivated without Strain XCand at the end of step (C-3), a blank supernatant SNC,Blankis obtained. Step (C-4) is repeated with the difference that 500 µl SNC,Blank is used instead of 500 µl of SNC. 15 Qualitative assessment of cellulase activity according to Assay C: Any Strain XC, the supernatant SNCof which shows a higher, preferably at least 10 % higher, more preferably at least 50 % higher, cellulase activity than SNC,Blankin step (C-4) of Assay C is, in particular, deemed to exhibit cellulase activity according to the invention. 20 VI.2.2 Assays D-I, D-II Assay D-I is the preferred quantitative test for determining the cellulase activity of a mutant of Bacillus velezensis DSM 34978 (hereinafter “Mutant 34978”) relative to the cellulase activity of Bacillus velezensis 25 DSM 34978. In Assay D-I, the following steps are carried out: (D-I-1) Steps (C-1) to (C-4) of Assay C are carried out, wherein Strain XC= Bacillus velezensis 30 DSM 34978. The cellulase activity in step (C-4) is measured and abbreviated as “HCI1”. Step (D-I-1) is repeated three times, and the average value of the three measurements of HCI1 is calculated and abbreviated as “ĤCI1”. (D-I-2) Steps (C-1) to (C-4) of Assay C are carried out, wherein Strain XC= Mutant 34978. The cellulase 35 activity in step (C-4) is measured and abbreviated as “HCI2”. Step (D-I-2) is repeated three times and the average value of the three measurements of HCI2 is calculated and abbreviated as “ĤCI2”. The percentage of cellulase activity ACellexhibited by the Mutant 34978 relative to Bacillus velezensis DSM 34978 is then calculated by ACell = (ĤCI2 / ĤCI1)*100. 40202400143 Foreign Filings 73 Assay D-II is the preferred quantitative test for determining the cellulase activity of a mutant of Bacillus velezensis DSM 34674 relative to the cellulase activity of Bacillus velezensis DSM 34674. In Assay D-II, the following steps are carried out: 5 (D-II-1) Steps (C-1) to (C-4) of Assay C are carried out, wherein Strain XC= Bacillus velezensis DSM 34674. The cellulase activity in step (C-4) is measured and abbreviated as “HCII1”. Step (D-II-1) is repeated three times and the average value of the three measurements of HCII1 is calculated and abbreviated as “ĤCII1”. 10 (D-II-2) Steps (C-1) to (C-4) of Assay C are carried out, wherein Strain XC= Mutant 34674. The area of the clearance zone obtained at the end of step (C-4) is measured and abbreviated as “HCII2”. Step (D-II-2) is repeated three times and the average value of the three measurements of HCII2is calculated and abbreviated as “ĤCII2”. 15 The percentage of cellulase activity ACell exhibited by the Mutant 34674 relative to Bacillus velezensis DSM 34674 is then calculated by ACell= (ĤCII2 / ĤCII1)*100. VI.3 Amylase activity: Assay E and Assays F-I, F-II: 20 “Amylase activity” in the sense of the present invention is deemed to be an activity that catalyzes the hydrolytic cleavage of a glycosidic bond within a polysaccharide such as starch (“glycosidic enzymatic activity”). 25 The prior art describes different assays to qualitatively and quantitatively determine amylase activity, for example in Oliveira et al., MethodsX 2019, 6, 246-258. Assay E is the preferred qualitative test for amylase activity according to the invention. 30 Whether a mutant of Bacillus velezensis DSM 34978 exhibits “amylase activity” is preferably determined by the following Assay E. Whether a mutant of Bacillus velezensis DSM 34674 exhibits “amylase activity” is preferably determined by the following Assay E. 35 In order to determine the amylase activity (in %) of a given mutant of Bacillus velezensis DSM 34978 relative to the amylase activity of Bacillus velezensis DSM 34978, Assay F-I is preferably used. In order to determine the amylase activity (in %) of a given mutant of Bacillus velezensis DSM 34674 40 relative to the amylase activity of Bacillus velezensis DSM 34674, Assay F-II is preferably used.202400143 Foreign Filings 74 VI.3.1 Assay E Assay E may be carried out by the following steps to determine whether a given Strain XE, for example Bacillus velezensis DSM 34978 or a given mutant of Bacillus velezensis DSM 34978, or Bacillus 5 velezensis DSM 34674 or a given mutant of Bacillus velezensis DSM 34674, exhibit amylase activity. (E-1) Strain XEis cultivated in 10 ml tryptic-soy-broth (“TSB”; Merck – 105459; peptone from casein 17.0 g / L; peptone from soymeal 3.0 g / L; D(+) glucose monohydrate 2.5 g / L; sodium chloride 5.0 g / L; di- potassium hydrogen phosphate 2.5 g / L), wherein the TSB medium further contained 2.5 g / L soluble 10 starch (Merck) at 37 °C and 200 rpm for 16 h. As inoculum, 20 µl of a cryo-conservation culture is used for each strain XE. (E-2) After the overnight cultivation, the optical density is measured at λ = 660 nm using a cuvette photometer and a culture volume for OD1 (in 1 ml) is obtained by centrifugation (5000 x g, 3 min, room 15 temperature). The filter-sterile supernatant (abbreviated as SNE) is obtained, adjusted (by dilution with TSB medium) to OD 1 and sterilized using a 0.2 µm filter and then used for the qualitative amylase test on specific selective agar plates [step (E-3)]. (E-3) Starch agar plates are prepared by using 37 g / L Luria-Bertani (“LB”) agar (Merck-110283) with 20 10 g / L soluble starch (Merck, CAS: 9005-84-9).5 µl of the supernatant SNE is dropped on the agar plates. (E-4) The plates are incubated at 37 °C for 24 h, and then flooded with 10 % Lugol’s solution (5 g iodine, 10 g potassium iodide in 10 ml distilled water), which is removed directly thereafter. The amylase activity is indicated by the extent (area) of the circular / elliptic clearance zone (also referred to as “halo of 25 degradation”). For the determination of the area of the clearance zone, the diameter (in case of a circular clearance zone) or the average value of the largest and smallest diameter (in case of an elliptic clearance zone) may be determined. Values are assessed in millimeters (mm) of two independent biological replicates. 30 (E-5) As blank control, step (E-1) is repeated except that no Strain XEis cultivated in TSB. The filter- sterile supernatant is diluted in the same ratio as in the case of the Strain XE in step (E-2) to be tested to give blank supernatant SNE,Blank. Then, step (E-3) is repeated with the difference that 5 µl of SNE,Blank is dropped on the agar plate prepared as described in step (E-3) and incubated for 24 h at 37 °C. 35 (E-6) Optionally, as further control and for quantification of the amylase activity, the area of a clearance zone may be compared to the area of a clearance zone of a pure α-amylase from Bacillus licheniformis (CAS: 9000-85-5) with an amylase activity of known quantity. For this, steps (E-3) and (E-4) are repeated, except that instead of 5 µl of SNE, 5 µl of a prepared solution of the α-amylase (0.1 mg / ml) is used. By this, the area size of a clearance zone may be correlated to a quantitative value of amylase activity. 40 Qualitative assessment of amylase activity according to Assay E:202400143 Foreign Filings 75 Any Strain XEthat shows visible amylase activity in step (E-4) of Assay E is, in particular, deemed to exhibit amylase activity according to the invention. Preferably, any Strain XEthat in step (E-4) shows a halo of degradation the area of which is larger, preferably at least 10 %, more preferably at least 50 % 5 larger, than the area of the clearance zone observed for SNE,Blankin step (E-5) is deemed to exhibit amylase activity. VI.3.2 Assays F-I, F-II Assay F-I is the preferred quantitative test for determining the amylase activity of a mutant of Bacillus 10 velezensis DSM 34978 (hereinafter “Mutant 34978”) relative to the amylase activity of Bacillus velezensis DSM 34978. In Assay F-I, the following steps are carried out: 15 (F-I-1) Steps (E-1) to (E-4) of Assay E are carried out, wherein Strain XE = Bacillus velezensis DSM 34978. The area of the clearance zone obtained at the end of step (E-4) is measured and abbreviated as “HEI1”. Step (F-I-1) is repeated three times and the average value of the three measurements of HEI1is calculated and abbreviated as “ĤEI1”. 20 (F-I-2) Steps (E-1) to (E-4) of Assay E are carried out, wherein Strain XE = Mutant 34978. The area of the clearance zone obtained at the end of step (E-4) is measured and abbreviated as “HEI2”. Step (F-I-2) is repeated three times and the average value of the three measurements of HEI2is calculated and abbreviated as “ĤEI2”. 25 The percentage of amylase activity AAmyexhibited by the Mutant 34978 relative to Bacillus velezensis DSM 34978 is then calculated by AAmy= (ĤEI2 / ĤEI1)*100. Assay F-II is the preferred quantitative test for determining the amylase activity of a mutant of Bacillus velezensis DSM 34674 relative to the amylase activity of Bacillus velezensis DSM 34674. 30 In Assay F-II, the following steps are carried out: (F-II-1) Steps (E-1) to (E-4) of Assay E are carried out, wherein Strain XE= Bacillus velezensis DSM 34674. The area of the clearance zone obtained at the end of step (E-4) is measured and 35 abbreviated as “HEII1”. Step (F-II-1) is repeated three times and the average value of the three measurements of HEII1 is calculated and abbreviated as “ĤEII1”. (F-II-2) Steps (E-1) to (E-4) of Assay E are carried out, wherein Strain XE= Mutant 34674. The area of the clearance zone obtained at the end of step (E-4) is measured and abbreviated as “HEII2”. Step (F-II-2)202400143 Foreign Filings 76 is repeated three times and the average value of the three measurements of HEII2is calculated and abbreviated as “ĤEII2”. The percentage of amylase activity AAmy exhibited by the Mutant 34674 relative to Bacillus velezensis 5 DSM 34674 is then calculated by AAmy= (ĤEII2 / ĤEII1)*100. VI.4 Lipase activity: Assays G, H “Lipase activity” in the sense of the present invention is deemed to be an activity that catalyzes the hydrolytic cleavage of an ester bond within triglycerides, diglycerides, and monoglycerides. 10 P. Chandra et al., Microb Cell Fact.2020, 19, 169 review the applications of microbial lipases, for example in waste water treatment and as cleaning agents. The prior art describes different assays to qualitatively and quantitatively determine lipase activity, for example in Guo et al., Enzyme and Microbial Technology 2015, 71, 8-12; Javed et al. Prog Biophys Mol 15 Biol.2018,132, 23-34 (doi: 10.1016 / j.pbiomolbio.2017.07.014.). Assay G is the preferred qualitative test for lipase activity according to the invention. Whether a mutant of Bacillus subtilis DSM 34981 exhibits “lipase activity” is preferably determined by the 20 following Assay G. A variety of para-nitrophenyl (“p-NP”) esters having two to 16 carbon atoms (p-NP acetate to p-NP palmitate) in their fatty acid side chain can be hydrolyzed by bacterial lipases (Javed et al., Progress in Biophysics and Molecular Biology 2018, 132, 23-34). In Assay G the lipase activity is measured by the amount of free p-NP which is the product of the hydrolysis of 4-nitrophenyloctanoate (“4-NP-C8”). In Assay G, free p-NP is directly measured via a photometric assay. 25 In order to determine the lipase activity (in %) of a given mutant of Bacillus subtilis DSM 34981 relative to the lipase activity of Bacillus subtilis DSM 34981, Assay H is preferably used. VI.4.1 Assay G 30 Assay G may be carried out by the following steps to determine whether a given Strain XG, for example a given mutant of Bacillus subtilis DSM 34981, exhibits lipase activity. (G-1) Strain XGis incubated in a pre-culture in 10 ml tryptic-soy-broth (“TSB”; Merck – 105459; peptone 35 from casein 17.0 g / L; peptone from soymeal 3.0 g / L; D(+) glucose monohydrate 2.5 g / L; sodium chloride 5.0 g / L; di-potassium hydrogen phosphate 2.5 g / L), at 37 °C and 200 rpm for 16 h. (G-2) After the incubation, the pre-culture is centrifugated twice and washed with main culture medium MCM0 (described in the context of Assay J). The main culture is incubated at 37 °C and 200 rpm 40 agitation for 4 hours. Afterwards, the culture is harvested by centrifugation (5000 x g, 3 min, room202400143 Foreign Filings 77 temperature) and adjusted to OD 0.25 (λ = 660 nm) in 180 µl 0.1 M Tris-buffer.180 µl of this suspension SBof bacterial cells is then used in step (G-4). (G-3) A stock solution S4NPC8 for the substrate of 4 mmol / L 4-nitrophenyloctanoate (“4-NP-C8”; Sigma- 5 Aldrich, CAS:1956-10-1) is prepared as follows: A solution of 4-NP-C8 in iso-propanol is prepared, and this stock solution is further diluted in 0.1 M Tris-buffer pH 8.5 to give S4NPC8as follows: 28.8 mg 4-NP-C8 are mixed with 6.25 ml iso-propanol, and 18.75 ml 0.1 M Tris-buffer (pH 8.5) are added. (G-4) 180 µl bacterial cell suspension SBis mixed with 20 µl S4NPC8in a 96-well microliter plate (Greiner 10 bio one, Ref.655101) and incubated at 25 °C for 60 min in a Tecan spark plate reader. The determination is carried out in the Tecan plate reader at λ = 410 nm. Every 2 min, a measurement is done and after 60 min, the final absorbance at λ = 410 nm is used for the evaluation. For the evaluation, a p-nitrophenol (“p-NP”) standard series (0 to 10 mmol / L) is prepared and used to 15 quantify the amount of released p-NP to determine the lipase activity in the Bacillus suspension SB. The activity of expressed lipase is given in mU / ml as mean value from two independent biological experiments. (G-5) For the determination of the baseline, a blank solution SG,blank of 20 µl substrate solution S4NPC8 in 20 180 µl 0.1 M Tris-buffer is used. As a positive control, different concentrations of a pure lipase from Candida rugosa (Sigma-Aldrich, L174) are used. Qualitative assessment of cellulase activity according to Assay G: 25 Any Strain XG, the suspension SBof which shows a higher, preferably at least 10 % higher, more preferably at least 50 % higher, lipase activity than SNG,Blank in step (G-4) of Assay G is, in particular, deemed to exhibit lipase activity according to the invention. 30 VI.4.2 Assay H Assay H is the preferred quantitative test for determining the lipase activity of a mutant of Bacillus subtilis DSM 34981 (hereinafter “Mutant 34981”) relative to the lipase activity of Bacillus subtilis DSM 34981. 35 In Assay H, the following steps are carried out: (H-1) Steps (G-1) to (G-4) of Assay G are carried out, wherein Strain XG= Bacillus subtilis DSM 34981. The lipase activity in step (G-4) is measured and abbreviated as “HH1”. Step (H-1) is repeated three times, and the average value of the three measurements of HH1 is calculated and abbreviated as “ĤH1”. 40202400143 Foreign Filings 78 (H-2) Steps (G-1) to (G-4) of Assay G are carried out, wherein Strain XG= Mutant 34981. The lipase activity in step (G-4) is measured and abbreviated as “HH2”. Step (H-2) is repeated three times and the average value of the three measurements of HH2is calculated and abbreviated as “ĤH2”. 5 The percentage of lipase activity ALipaexhibited by the Mutant 34981 relative to Bacillus subtilis DSM 34981 is then calculated by ALipa= (ĤH2 / ĤH1)*100. VI.5 Valeric acid metabolism rate and ability to grow on valeric acid (1000 ppm): Assay J VI.5.1 Assay J 10 Assay J allows to determine two different properties of a given strain, namely 1) A strain’s ability to grow in the presence of a certain concentration of VA (exemplified in Assay J on the basis of a concentration of 1000 ppm VA). This ability to grow is expressed as factor ΓXJ, which is positive for those strains that are deemed to be able to grow on VA with a certain 15 concentration; 2) The ability to reduce VA of a certain maximal concentration (exemplified in Assay J on the basis of a concentration of 1000 ppm VA). This ability to reduce VA may then be quantified by a constant kXJ, wherein kXJ≤ 1. 20 VI.5.1.1 y to grow on valeric acid, factor ΓXJ Assay J may be carried out by the following steps to determine whether a given Strain XJ, for example B. velezensis DSM 34978 or a given mutant of B. velezensis DSM 34978, B. velezensis DSM 34674 or a given mutant of B. velezensis DSM 34674, Bacillus licheniformis DSM 34977 or a given mutant of 25 Bacillus licheniformis DSM 34977, Priestia megaterium DSM 34980 or a given mutant of Priestia megaterium DSM 34980, Bacillus subtilis DSM 34981 or a given mutant of Bacillus subtilis DSM 34981, grows on valeric acid of a certain concentration xVA, in particular of a concentration xVA of 1000 ppm. The concentration of valeric acid in the medium MCM+Valthat is used in Assay J is xVA= 1000 ppm. 30 Thus, Assay J allows to determine whether a given Strain X is able to grow in the presence of 1000 ppm VA. “Able to grow in the presence of 1000 ppm VA” may be abbreviated as “to grow on 1000 ppm valeric acid” or “to grow on valeric acid (1000 ppm)”. In order to determine the ability to grow at lower or higher, in particular higher, concentrations xVAof VA 35 (for example xVA = 5000 ppm), Assay J is easily adapted by substituting MCM+Val by another medium MCM*+Val which is identical to MCM+Val, but has a lower or higher, in particular higher, concentration xVA of VA. For example, for xVA= 5000 ppm, a medium MCM*+Valwith 5000 ppm VA may be used which is obtained by the same procedure as stated below for MCM+Val, except that in step 5., 5 g valeric acid are deployed.202400143 Foreign Filings 79 If such medium MCM*+Valis used in Assay J, Assay J allows to determine whether a given Strain X is able to grow in the presence of 5000 ppm VA. “Able to grow in the presence of 5000 ppm VA” may be abbreviated as “to grow on 5000 ppm valeric acid” or “to grow on valeric acid (5000 ppm)”. 5 The same applies, logically, to any other variation of Assay J where yet another medium MCM**+Valwith a yet different concentration xVAof VA is used. The skilled person knows that such medium is simply obtained by the same procedure as described for MCM+Val, by simply adjusting the amount of VA used in step 5. 10 VI.5.1.2 Rate of metabolization of valeric acid, constant kXJAssay J may furthermore be carried out by the following steps to determine whether a given Strain XJ, for example B. velezensis DSM 34978 or a given mutant of B. velezensis DSM 34978, B. velezensis DSM 34674 or a given mutant of B. velezensis DSM 34674, Bacillus licheniformis DSM 34977 or a given 15 mutant of Bacillus licheniformis DSM 34977, Priestia megaterium DSM 34980 or a given mutant of Priestia megaterium DSM 34980, Bacillus subtilis DSM 34981 or a given mutant of Bacillus subtilis DSM 34981 is able to metabolize (and thus reduce) valeric acid of a certain concentration xVA, in particular a concentration of xVA= 1000 ppm. 20 The concentration of valeric acid in the medium MCM+Val that is used in Assay J is xVA = 1000 ppm. Thus, Assay J allows to determine the ability to metabolize valeric acid of a given Strain X, wherein the concentration of VA is xVA= 1000 ppm. “Ability to metabolize valeric acid […], wherein the concentration of VA is 1000 ppm” may be abbreviated as “able to metabolize 1000 ppm valeric acid” or “able to metabolize valeric acid (1000 ppm)”. 25 In order to determine the ability to metabolize VA at lower or higher, in particular higher, concentrations xVA of VA (for example xVA = 5000 ppm), Assay J is easily adapted by substituting MCM+Val by another medium MCM*+Val which is identical to MCM+Val, but has a lower or higher, in particular higher, concentration xVAof VA. For example, for xVA= 5000 ppm, a medium MCM*+Valwith 5000 ppm VA may 30 be used which is obtained by the same procedure as stated below for MCM+Val, except that in step 5., 5 g valeric acid are deployed. If such medium MCM*+Valis used in Assay J, Assay J allows to determine whether a given Strain X is able to metabolize 5000 ppm VA. “Ability to metabolize valeric acid […], wherein the concentration of VA 35 is 5000 ppm” may be abbreviated as “able to metabolize 5000 ppm valeric acid” or “able to metabolize valeric acid (5000 ppm)”. The same applies, logically, to any other variation of Assay J where yet another medium MCM**+Valwith a yet different concentration xVA is used. The skilled person knows that such medium is simply obtained 40 by the same procedure as described for MCM+Val, by simply adjusting the amount of VA used in step 5.202400143 Foreign Filings 80 VI.5.1.3 Steps according to Assay J The following culture media MCM+Valand MCM0are prepared: 5 MCM+Valis a main culture medium containing valeric acid obtained by combining the following solutions / substances: 1. 200 g aqueous salt solution 1 with 20 g / L KH2PO4, 61 g / L K2HPO4, 16 g / L (NH4)2SO4; 2. 10 g aqueous salt solution 2 with 0.176 g / L Mn(II)SO4*H2O and 12.3 g / L MgSO4*H2O; 3. 10 g of an aqueous ammonium iron (III) citrate solution with a concentration of 2.2 g / L of 10 ammonium iron (III) citrate; 4. 20 g of a 50 % (w / v) aqueous glucose monohydrate solution (50 g glucose monohydrate are dissolved in water to give a final volume of aqueous solution of 100 ml); 5. 1 g valeric acid (Sigma-Aldrich, 240370). 15 The stocks 1. to 5. are combined and filled up to 1 L; the pH is adjusted to 7. MCM0is a main culture medium containing no valeric acid obtained by combining the stocks 1. to 4. and filling them up to 1 L; the pH is adjusted to 7. 20 In Assay J, the following steps are carried out: (J-1) Strain XJis incubated in a pre-culture PCJin 10 ml tryptic-soy-broth [“TSB”; Merck – 105459; peptone from casein 17.0 g / L; peptone from soymeal 3.0 g / L; D(+) glucose monohydrate 2.5 g / L; sodium chloride 5.0 g / L; di-potassium hydrogen phosphate 2.5 g / L]. PCJ is then divided one half each, PCJ+ and 25 PCJ-. (J-2) PCJ+ and PCJ- are each centrifugated and the respective pellet is redispersed in aqueous 0.9 % (w / v) NaCl solution (“aqueous 0.9 % (w / v) NaCl solution” means that 0.9 g NaCl are dissolved in water to give a final volume of aqueous solution of 100 ml). Then, each dispersion is centrifugated for 30 5 min at 5000 x g and the NaCl solution is removed from the obtained pellet (1stwashing). (J-3) Each pellet is redispersed in fresh aqueous 0.9 % (w / v) NaCl solution. Then, each dispersion is centrifugated for 5 min at 5000 x g and the NaCl solution is removed (2ndwashing). The pellet from PCJ+is used in step (J-4). The pellet from PCJ-is used in step (J-5). 35 (J-4) The washed pellet from PCJ+ from step (J-3) is diluted with main culture medium MCM+Val until an OD of 0.1 at λ = 660 nm (νStart= OD 0.1). MCM+Valcontains valeric acid (Sigma-Aldrich, 240370) in a concentration of c0= 1 g / L. The incubation is at 30 °C with 225 rpm for 48 h in a small cultivation system (Woulter-Deutz). Then, the OD at λ = 660 nm is measured (“ν+Val”). Then, the culture is centrifugated at 40 13000 x g for 3 minutes at room temperature (“RT”) and subsequently the supernatant SN+Val is harvested. The concentration c+Valof valeric acid in SN+Valis quantified using an analytical method.202400143 Foreign Filings 81 (J-5) The washed pellet from PCJ-from step (J-3) is diluted with main culture medium MCM0until an OD of 0.1 at λ = 660 nm (νStart= OD 0.1). MCM0comprises no valeric acid. The incubation is at 30 °C with 225 rpm for 48 h in a small cultivation system (Woulter-Deutz). Then, the OD at λ = 660 nm is measured 5 (“ν-Val”). Then, the culture is centrifugated at 13000 x g for 3 minutes at RT and subsequently the supernatant SN-Valis harvested. The concentration c-Valof valeric acid in SN-Valis quantified using an analytical method (this may be made as a control and / or standardization, since the concentration should be c-Val= 0). 10 (J-6) For a blank control, the same volume of main culture medium MCM+Valas in step (J-4), but without Strain XJ, is incubated at 30 °C with 225 rpm for 48 h in a small cultivation system (Woulter-Deutz). Then, the culture medium is centrifugated at 13000 x g for 3 minutes at RT and subsequently the supernatant SNBlankis harvested. The concentration cVal0of valeric acid in SNBlankis quantified using an analytical method as a control. 15 VI.5.1.4 Evaluation of Assay J VI.5.1.4.1 …at 1000 ppm VA Where Assay J is carried out with MCM+Val, namely a concentration of valeric acid of xVA = 1000 ppm, the 20 following evaluation may be made: → If ν+Valis higher than ν-Val, then XJis deemed to grow on 1000 ppm valeric acid according to the invention. The improved growth of XJ on valeric acid medium (1000 ppm) may then be expressed as factor ΓXJ; 1000 ppm = ν+Val / ν-Val. In particular, according to the invention, in order for a strain XJ to be able 25 to grow on valeric acid medium (1000 ppm), the condition ΓXJ; 1000 ppm> 1 is fulfilled. → If the concentration of valeric acid c+Val in SN+Val is lower than the concentration of valeric acid cVal0 in SNBlank, then XJ is able to metabolize valeric acid (1000 ppm). The rate of metabolization of valeric acid (1000 ppm) by XJmay then be expressed as constant kXJ; 1000 ppm= 1 – c+Val / cVal0. 30 The effectiveness ΕXJ; 1000 ppm to reduce valeric acid (1000 ppm) of a strain XJ, in particular a strain XJ which fulfills the condition “ΓXJ; 1000 ppm > 1”, may then be expressed as the ratio ΕXJ; 1000 ppm as follows: ΕXJ; 1000 ppm= kXJ; 1000 ppm* ΓXJ; 1000 ppm. VI.5.1.4.2 …at 5000 ppm VA 35 Where Assay J is carried out with another medium MCM*+Val instead of MCM+Val, namely at a concentration of valeric acid of xVA= 5000 ppm, the following evaluation may be made:202400143 Foreign Filings 82 → If ν+Valis higher than ν-Val, then XJis deemed to grow on 5000 ppm valeric acid according to the invention. The improved growth of XJon valeric acid medium (5000 ppm) may then be expressed as factor ΓXJ; 5000 ppm= ν+Val / ν-Val. In particular, according to the invention, in order for a strain XJto be able to grow on valeric acid medium (5000 ppm), the condition ΓXJ; 5000 ppm > 1 is fulfilled. 5 → If the concentration of valeric acid c+Valin SN+Valis lower than the concentration of valeric acid cVal0in SNBlank, then XJis able to metabolize valeric acid (5000 ppm). The rate of metabolization of valeric acid (5000 ppm) by XJ may then be expressed as constant kXJ; 5000 ppm = 1 – c+Val / cVal0. 10 The effectiveness ΕXJ; 5000 ppmto reduce valeric acid (5000 ppm) of a strain XJ, in particular a strain XJwhich fulfills the condition “ΓXJ; 5000 ppm> 1”, may then be expressed as the ratio ΕXJ; 5000 ppmas follows: ΕXJ; 5000 ppm= kXJ; 5000 ppm* ΓXJ; 5000 ppm. 15 VI.5.1.4.3 …at a general concentration of VA, i.e. xVA Where Assay J is carried out with another medium MCM**+Valinstead of MCM+Val, namely at a concentration of valeric acid of xVA, the following evaluation may be made: 20 → If ν+Val is higher than ν-Val , then XJ is deemed to grow at xVA valeric acid according to the invention. The improved growth of XJon valeric acid medium (xVA) may then be expressed as factor ΓXJ;xVA= ν+Val / ν-Val. In particular, according to the invention, in order for a strain XJto be able to grow on valeric acid medium (xVA), the condition ΓXJ;xVA > 1 is fulfilled. 25 → If the concentration of valeric acid c+Valin SN+Valis lower than the concentration of valeric acid cVal0in SNBlank, then XJis able to metabolize valeric acid (xVA). The rate of metabolization of valeric acid (xVA) by XJ may then be expressed as constant kXJ; xVA = 1 – c+Val / cVal0. The effectiveness ΕXJ;XVAto reduce valeric acid (xVA) of a strain XJ, in particular a strain XJwhich fulfills 30 the condition “ΓXJ;xVA> 1”, may then be expressed as the ratio ΕXJ;XVAas follows: ΕXJ;XVA = kXJ; xVA* ΓXJ; xVA. VI.5.1.5 Analysis of VA concentrations in the context of Assay J 35 In Assay J, the quantification of valeric acid are done by an analytical method as follows: The respective sample and a series of calibration standards are mixed with an internal standard (2-methylhexanoic acid). An excess of NaCl is added to the sample, and it is then diluted with 1 part 40 50 wt.-% sulfuric acid to 4 parts sample. The resulting mixture is extracted in a ratio of 1 part diethyl ether202400143 Foreign Filings 83 to 1.25 parts sample for 10 minutes and then centrifuged for 10 minutes at 3000 g. The organic supernatant is removed and, if necessary, further diluted to a concentration range of 1 g / L. Samples and calibration standards are measured using an Agilent GC 8860 equipped with split / spitless injector and FID detector on a GC column (BP2130m; ID 0.32 mm; film 0.25 μm) at a flow rate of 1 ml / min He. The 5 separation is carried out by means of a temperature gradient from 130 °C to 180 °C within 8.5 min. The chromatograms are evaluated by means of a multi-point area evaluation linear without zero crossing with 2-methylhexanoic acid as the internal standard. Valeric acid is eluting at 5.4 min within the program. VI.5.2 Assays K-I, K-II, K-III VI.5.2.1 Assay K-I 10 is the preferred quantitative test for determining the effectiveness ΕXJ% (xVA) to reduce valeric acid of a mutant of Bacillus licheniformis DSM 34977 (hereinafter “Mutant 34977”) relative to the effectiveness to reduce valeric acid of Bacillus licheniformis DSM 34977, which may be determined for a given concentration xVA, in particular of a concentration xVA= 1000 ppm or a concentration 15 xVA = 5000 ppm. In Assay K-I, the following steps are carried out: (K-I-1) Steps (J-1) to (J-5) of Assay J are carried out for a given concentration xVA, in particular a 20 concentration xVA = 1000 ppm or a concentration xVA = 5000 ppm, wherein Strain XJ = Bacillus licheniformis DSM 34977. Step (K-I-1) is repeated three times, and the average value of the three measurements of ΕXJ= ΓXJ*kXJis calculated and abbreviated as “ÊKI1”. (K-I-2) Steps (J-1) to (J-5) of Assay J are carried out for a given concentration xVA, in particular a 25 concentration xVA= 1000 ppm or a concentration xVA= 5000 ppm, wherein Strain XJ= mutant of Bacillus licheniformis DSM 34977. Step (K-I-2) is repeated three times, and the average value of the three measurements of ΕXJ = ΓXJ *kXJ is calculated and abbreviated as “ÊKI2”. The effectiveness ΕXJ%(xVA) exhibited by the Mutant 34977 to reduce valeric acid relative to the 30 effectiveness of Bacillus licheniforms DSM 34977 to reduce valeric acid for a given concentration xVAis then calculated by ΕXJ% (xVA) = (ÊKI2 / ÊKI1)*100. VI.5.2.2 Assay K-II 35 is the preferred quantitative test for determining the effectiveness ΕXJ% (xVA) to reduce valeric acid of a mutant of Priestia megaterium DSM 34980 (hereinafter “Mutant 34980”) relative to the effectiveness to reduce valeric acid of Priestia megaterium DSM 34980, which may be determined for a202400143 Foreign Filings 84 given concentration xVA, in particular of a concentration xVA= 1000 ppm or a concentration xVA= 5000 ppm. In Assay K-II, the following steps are carried out: 5 (K-II-1) Steps (J-1) to (J-5) of Assay J are carried out for a given concentration xVA, in particular a concentration xVA= 1000 ppm or a concentration xVA= 5000 ppm, wherein Strain XJ= Priestia megaterium DSM 34980. Step (K-II-1) is repeated three times, and the average value of the three measurements of ΕXJ= ΓXJ*kXJis calculated and abbreviated as “ÊKII1”. 10 (K-II-2) Steps (J-1) to (J-5) of Assay J are carried out for a given concentration xVA, in particular a concentration xVA = 1000 ppm or a concentration xVA = 5000 ppm, wherein Strain XJ = mutant of Priestia megaterium DSM 34980. Step (K-II-2) is repeated three times, and the average value of the three measurements of ΕXJ= ΓXJ*kXJis calculated and abbreviated as “ÊKII2”. 15 The effectiveness ΕXJ% exhibited by the Mutant 34980 to reduce valeric acid relative to the effectiveness of Priestia megaterium DSM 34980 to reduce valeric acid for a given concentration xVAis then calculated by ΕXJ%= (ÊKII2 / ÊKII1)*100. VI.5.2.3 Assay K-III 20 is the preferred quantitative test for determining the effectiveness ΕXJ%(xVA) to reduce valeric acid of a mutant of Bacillus subtilis DSM 34981 (hereinafter “Mutant 34981”) relative to the effectiveness to reduce valeric acid of Bacillus subtilis DSM 34981, which may be determined for a given concentration 25 xVA, in particular of a concentration xVA= 1000 ppm or a concentration xVA= 5000 ppm. In Assay K-III, the following steps are carried out: 30 (K-III-1) Steps (J-1) to (J-5) of Assay J are carried out for a given concentration xVA, in particular a concentration xVA = 1000 ppm or a concentration xVA = 5000 ppm, wherein Strain XJ = Bacillus subtilis DSM 34981. Step (K-III-1) is repeated three times, and the average value of the three measurements of ΕXJ= ΓXJ*kXJis calculated and abbreviated as “ÊKIII1”. 35 (K-III-2) Steps (J-1) to (J-5) of Assay J are carried out for a given concentration xVA, in particular a concentration xVA = 1000 ppm or a concentration xVA = 5000 ppm, wherein Strain XJ = mutant of Bacillus subtilis DSM 34981. Step (K-III-2) is repeated three times, and the average value of the three measurements of ΕXJ= ΓXJ*kXJis calculated and abbreviated as “ÊKIII2”.202400143 Foreign Filings 85 The effectiveness ΕXJ%(xVA) exhibited by the Mutant 34981 to reduce valeric acid relative to the effectiveness of Bacillus subtilis DSM 34981 to reduce valeric acid for a given concentration xVAis then calculated by ΕXJ%(xVA) = (ÊKIII2 / ÊKIII1)*100. 5 VI.5.3 Assays L-I, L-II VI.5.3.1 Assay L-I is the preferred quantitative test for determining kXJ%(xVA) i.e. the metabolization rate of a 10 valeric acid medium of a mutant of Bacillus velezensis DSM 34978 (hereinafter “Mutant 34978”) relative to the metabolization rate of a valeric acid medium of Bacillus velezensis DSM 34978, which may be determined for a given concentration xVA, in particular for a concentration xVA = 1000 ppm or a concentration xVA= 5000 ppm. 15 In Assay L-I, the following steps are carried out: (L-I-1) Steps (J-1) to (J-4) and (J-6) of Assay J are carried out for a given concentration xVA, in particular a concentration xVA= 1000 ppm or a concentration xVA= 5000 ppm, wherein Strain XJ= Bacillus velezensis DSM 34978. Step (L-I-1) is repeated three times, and the average value of the three 20 measurements of kXJ is calculated and abbreviated as “κLI1”. (L-I-2) Steps (J-1) to (J-4) and (J-6) of Assay J are carried out for a given concentration xVA, in particular a concentration xVA = 1000 ppm or a concentration xVA = 5000 ppm, wherein Strain XJ = mutant of Bacillus velezensis DSM 34978. Step (L-I-2) is repeated three times, and the average value of the three 25 measurements of kXJis calculated and abbreviated as “κLI2”. The relative metabolization rate kXJ% (xVA) of valeric acid for a given concentration xVA exhibited by the Mutant 34978 relative to the metabolization of valeric acid of Bacillus velezensis DSM 34978 is then calculated by kXJ%(xVA) = (κLI2 / κLI1)*100. 30 VI.5.3.2 Assay L-II is the preferred quantitative test for determining kXJ% (xVA) i.e. the metabolization rate of a valeric acid medium of a mutant of Bacillus velezensis DSM 34674 (hereinafter “Mutant 34674”) relative to the metabolization rate of a valeric acid medium of Bacillus velezensis DSM 34674, which may be 35 determined for a given concentration xVA, in particular for a concentration xVA = 1000 ppm or a concentration xVA = 5000 ppm. In Assay L-II, the following steps are carried out:202400143 Foreign Filings 86 (L-II-1) Steps (J-1) to (J-4) and (J-6) of Assay J are carried out for a given concentration xVA, in particular a concentration xVA= 1000 ppm or a concentration xVA= 5000 ppm, wherein Strain XJ= Bacillus velezensis DSM 34674. Step (L-II-1) is repeated three times, and the average value of the three measurements of kXJ is calculated and abbreviated as “κLII1”. 5 (L-II-2) Steps (J-1) to (J-4) and (J-6) of Assay J are carried out for a given concentration xVA, in particular a concentration xVA= 1000 ppm or a concentration xVA= 5000 ppm, wherein Strain XJ= mutant of Bacillus velezensis DSM 34674. Step (L-II-2) is repeated three times, and the average value of the three measurements of kXJis calculated and abbreviated as “κLII2”. 10 The relative metabolization rate of valeric acid kXJ%(xVA) exhibited by the Mutant 34674 relative to the metabolization of valeric acid for a given concentration xVA of Bacillus velezensis DSM 34674 is then calculated by kXJ%(xVA) = (κLII2 / κLII1)*100. 15202400143 Foreign Filings 87 Examples Examples I. to III. show advantageous enzymatic activities of Bacillus and Priestia strains which may advantageously be used in cleaning where metabolization of different substrates underlies the cleaning 5 effect. They may also be used in a method of feeding animals, for example where the metabolization of different substrates is used to fatten livestock. Preferably, they are used in cleaning. Example IV. shows the surprising properties of the different bacterial species and strains in terms of positive or negative growth rate in presence of VA and VA reduction rate. The surprising findings described in Example II. for Priestia megaterium DSM 34980 undergird the 10 present invention. I. Determination of protease, amylase, and cellulase activity of Bacillus velezensis DSM 34978 and DSM 34674 Six different Bacillus velezensis strains (i.e. DSM 34978, DSM 34674, prior art strain DSM 33857 as well 15 as three commercial Bacillus velezensis strains), one Bacillus licheniformis strain DSM 13, and one Priestia megaterium DSM 33356 were tested for protease, amylase and cellulase activity in a testing procedure according to Assay A-I, Assay E, and Assay C, respectively. The protease activity tested in Assay A-I is protease activities in the supernatant, i.e. secreted protease activity. Two Bacillus velezensis strains DSM 34978 and DSM 34674 were isolated from the soil, respectively. 20 Three further Bacillus velezensis strains (abbreviated as “Bacillus velezensis strain 1”, “Bacillus velezensis strain 2”, and “Bacillus velezensis strain 3”, respectively) were isolated from commercially available cleaning products A, B, and C, respectively, and investigated as comparisons. DSM 33857 is a prior art Bacillus velezensis strain (disclosed in EP 4130258 A1). DSM 33356 is a prior art Priestia megaterium strain (disclosed in WO 2021 / 129998 A1). DSM 13 is a prior art Bacillus licheniformis strain 25 (disclosed in B. Veith et al., J Mol Microbiol Biotechnol 2004, 7, 204-211). The protease and amylase activity of each of these strains was assessed in two test series, series A and series B. The cellulase activity of each of these strains was assessed in test series A.30 The testing for protease activity was carried out as follows: Each of the strains of interest was cultivated in 10 ml tryptic-soy-broth [TSB; Merck - 105459 (peptone from casein 17.0 g / L; peptone from soymeal 3.0 g / L; D (+) glucose monohydrate 2.5 g / L; sodium chloride 5.0 g / L; di-potassium hydrogen phosphate 2.5 g / L)] at 37 °C and 200 rpm overnight (16 h) separately. As 35 inoculum, 20 µl of a cryo-conservation culture was used for each strain. After the overnight cultivation, the optical density was measured at λ = 660 nm using a cuvette photometer and a culture volume for OD 1 (in 1 ml) was adjusted by centrifugation (5000 x g, 3 min, room temperature). The filter-sterile supernatant (previously adjusted to OD1) was used for the qualitative protease test on specific selective agar plates.202400143 Foreign Filings 88 10 % Crossley milk agar (CM0213, Oxoid; 10 g / L skim milk powder, 1 g / L peptone, 0.01 g / L bromocresol purple, 13 g / L agar-agar) was prepared and 5 µl of the supernatant of each strain of interest was dropped on the agar plates. After an incubation at 37 °C for 24 h, the protease activity was indicated by a clearance zone (“halo of degradation”), which was measured and compared to a pure protease from 5 Bacillus licheniformis (subtilisin, P5380, Sigma-Aldrich) concentrated to 1 mg / ml. Through the indicator dye in the agar medium, the elucidation by protease degradation is directly visible. The clearance zone is given as an average of the horizontal and vertical diameters. Values are given in millimeters (mm) of two independent biological replicates. 10 Two test series were performed. In the first test series A, the protease activity of Priestia megaterium DSM 33356, Bacillus licheniformis DSM 13, and Bacillus velezensis strains DSM 34978, DSM 34674, as well as Bacillus velezensis strains 1 to 3 was determined. The results are summarized in table 1-A. In the second test series B , the protease activity of Bacillus velezensis strains DSM 34978, DSM 34674, and DSM 33857 was determined. The results are summarized in table 1-B. 15202400143 Foreign Filings 89 I.2 Determination of the amylase activity Like the protease activity test, the amylase activity was also checked in a qualitative plate test. 5 The strains of interest were cultivated in 10 ml tryptic-soy-broth with soluble starch [TSB; Merck- 105459 (peptone from casein 17.0 g / L; peptone from soymeal 3.0 g / L; D(+)glucose monohydrate 2.5 g / L; sodium chloride 5.0 g / L; di-potassium hydrogen phosphate 2.5 g / L) + 2.5 g / L soluble starch (Merck) at 37 °C and 200 rpm overnight (16 h) separately. As inoculum, 20 µl of a cryo-conservation culture was used for each strain. After the overnight cultivation, the optical density was measured at λ = 660 nm using a cuvette 10 photometer and a culture volume for OD1 (in 1ml) was adjusted by centrifugation (5000 x g, 3 min, room temperature). The filter-sterile supernatant (previously adjusted to OD1 and sterilized using a 0.2 µm filter) was used for the qualitative amylase test on specific selective agar plates. Starch agar plates were prepared by using 37 g / L Luria-Bertani (“LB”) agar (Merck-110283) with10 g / L 15 soluble starch (Merck, CAS: 9005-84-9).5 µl of the supernatant of each strain were dropped on the agar plate. Plates were incubated at 37 °C for 24 h. The α-amylase from Bacillus licheniformis (CAS: 9000-85-5) was used as control.5 µl of a prepared 0.1 mg / ml solution was dropped similarly. Specifically, the amylase activity was observed as a clear zone around the bacterial supernatant spots or the α-amylase spot, becoming evident after application of 10 ml of 10 % Lugol’s solution (5 g iodine, 10 g 20 potassium iodide in 10 ml distilled water) to the plate. After removing the Lugol’s solution, the diameter of the clearance zones was measured horizontally and vertically, and the mean thereof used for determining the area of the clearance zone. The test is performed in two independent biological replicates. The results are summarized in table 1. 25 Two test series were performed. In the first test series A, the amylase activity of Priestia megaterium DSM 33356, Bacillus licheniformis DSM 13, and Bacillus velezensis strains DSM 34978, DSM 34674, as well as Bacillus velezensis strains 1 to 3 was determined. The results obtained in test series A are summarized in table 1-A. In the second test series B, the amylase activity of Bacillus velezensis strains DSM 34978, DSM 34674, 30 and DSM 33857 was determined. The results obtained in test series B are summarized in table 1-B. I.3 Determination of the cellulase activity The cell free supernatant of the Bacillus / Priestia strains of interest was tested regarding cellulase 35 activity. Cellulase activity produced by the different Bacillus / Priestia strains of interest and released in the supernatant was quantified with the EnzChek® Cellulase kit from Molecular Probes / life technologies (E33953) following the working protocol. The principle of this test is based on the cellulase-catalyzed conversion of the substrate EnzChek® Cellulase Substrate, blue fluorescent, 339 / 452, whereby the fluorescence is enhanced. 40202400143 Foreign Filings 90 The supernatant was prepared beforehand. A pre-culture of each strain of interest was done in 10 ml VIB medium (Difco Veal Infusion Broth, Ref.234420) at 37 °C and 200 rpm overnight (16 h). After the incubation, a new main culture with 2.5 ml CMC Growth Medium [minimal-salt medium with 10 g / L carboxymethyl cellulose (Sigma 419311)] was inoculated with 125 µl pre-culture using a small deep-well 5 incubation plate and incubated at 37 °C for 24 h at 300 rpm. After 24 hours, the OD at λ = 660 nm of each culture was measured and the supernatant harvested by centrifugation. This was done with a 1 ml aliquot of each culture in a 1.5 ml Eppendorf tube for 5 min at 13000 rpm. After that, approx.500 µl of culture supernatant was used for the enzyme test. 10 The detection limit of the cellulase kit was determined as 4mU-3U / ml activity. Therefore, a 2U / ml cellulase from Aspergillus niger (Sigma-Aldrich, C1184) and dilutions were prepared for a standard curve for quantification. The assay was done according to the kit manual. The measurement was performed in black 96-well microtiter plates (Greiner FIA-Plate, black 96K, F-form, 655076-225) and in the Tecan plate reader infinite M1000 Pro. Subsequently, the fluorescence was measured at an excitation of λ = 339 nm 15 and an emission of λ = 452 nm. The cellulase activity was calculated based on the standard curve and the activity was normalized to OD 1 (λ = 660 nm) to standardize over cell growth differences after 24 hours incubation. One test series A was performed. The cellulase activity of Priestia megaterium DSM 33356, Bacillus 20 velezensis strains DSM 33857, DSM 34978, DSM 34674, and Bacillus velezensis strains 1 to 3 was determined. The results are summarized in table 1-A. I.4 Results 25 The results obtained in test series A are summarized in the following table 1-A: Table 1-A: Protease and amylase activities in supernatants (“SN”) measured via a qualitative plate assay by determining the halo of degradation size (Ø in mm). Cellulase activity of supernatants is given as quantitative values in mU / OD1. The experiments were performed in two biological replicates and the 30 means and standard deviations (“σ”) are given. Comparative strains 1, 2, 3 from product A, B and C, respectively, belong to the Bacillus species velezensis. Strains DSM 34978 and DSM 34674 belong to the Bacillus species velezensis. DSM 33857 is a prior art Bacillus velezensis strain (disclosed in EP 4130258 A1). DSM 33356 is a prior art Priestia megaterium strain (disclosed in WO 2021 / 129998 A1). DSM 13 is a prior art Bacillus licheniformis strain (disclosed in B. Veith et al., J Mol 35 Microbiol Biotechnol 2004, 7, 204-211) (“n.d.” = not determined; “n.d.*” = not determined in test series A; but determined in test series B). Strain Protease activity SN Amylase activity SN Cellulase activity SN Ø halo of degradation [mm] Ø halo of degradation [mm] mU / OD 1202400143 Foreign Filings 91 16.97 7.54 1660.76 DSM 34978 (σ 0.32) (σ 0.58) (σ 440.15) 15.89 7.34 1084.81 DSM 34674 (σ 0.32) (σ 1.26) (σ 153.33) 12.9 7.50 944.01 Strain 1 (σ 0.765) (σ 1.96) (σ 271.23) 14.30 5.99 764.29 Strain 2 (σ 0.53) (σ 0.75) (σ 113.04) 13.74 7.50 751.43 Strain 3 (σ 0.18) (σ 0.45) (σ 77.52) 1340.49 DSM 33857 n.d.* n.d.* (σ 14.06) DSM 33356 - - - DSM 13 - - n.d. The results obtained in test series B are summarized in the following table 1-B: Table 2-B: Protease and amylase activities in supernatants (“SN”) measured via a qualitative plate assay 5 by determining the halo of degradation size (Ø in mm). The experiments were performed in two biological replicates and the means and standard deviations (“σ”) are given. Strains DSM 34978 and DSM 34674 belong to the Bacillus species velezensis. DSM 33857 is a prior art Bacillus velezensis strain (disclosed in EP 4130258 A1). Strain Protease activity SN Amylase activity SN Ø halo of degradation [mm] Ø halo of degradation [mm] DSM 34978 14.30 (σ 0.28) 10.255 (σ 0.035) DSM 34674 14.01 (σ 0.33) 8.875 (σ 0.23) DSM 33857 12.98 (σ 0.01) 10.13 (σ 0.38) 10 I.4.1 Protease Activities The results obtained in test series A, summarized in table 1-A, show the following: Bacillus velezensis strains DSM 34978 and DSM 34674 showed remarkably high activity for protease 15 compared to the other screened Bacillus / Priestia strains. As described under point I.1, the supernatants were harvested from a culture of each strain and adjusted to an optical density of OD1 to standardize over growth effects. The degradation or clearance zones, measured as the diameter (“Ø”) in mm, have a Ø size of 16.97 mm and 15.89 mm for DSM 34978 and DSM 34674, respectively. Comparative Bacillus velezensis strains 1, 2, and 3 were tested in the same way and it could be shown that the protease202400143 Foreign Filings 92 activity of all of these strains was lower (see table 1-A; Ø sizes of 12.9 mm, 14.30 mm, and 13.74 mm, respectively). As a further control, the protease activity of two different species from the prior art was tested: Priestia megaterium DSM 33356 and Bacillus licheniformis DSM 13. Neither strain showed any protease activity. 5 The results obtained in test series B, summarized in table 1-B, show the following: Bacillus velezensis strains DSM 34978 and DSM 34674 also showed remarkably higher activity for protease compared to the prior art Bacillus velezensis strain DSM 33857. As described under point I.1, 10 the supernatants were harvested from a culture of each strain and adjusted to an optical density of OD 1 to standardize over growth effects. The degradation or clearance zones, measured as the diameter (“Ø”) in mm, have a Ø size of 14.30 mm and 14.01 mm for DSM 34978 and DSM 34674, respectively. Bacillus velezensis strain DSM 33857 gave a smaller Ø size of 12.98 mm. 15 It was hence surprisingly found that DSM 34978 and DSM 34674 supernatants contained the highest levels of proteases which can degrade casein and whey proteins very effectively. These halo sizes were compared to the halo of a pure protease from Bacillus licheniformis with an activity of 7-15 U / mg. The 5 µl of the 1 mg / ml solutions have a calculated activity of around 35-75 µU, that is represented by a degradation halo Ø size of 22.12 mm. 20 The qualitative plate assay hence showed that the two Bacillus velezensis strains DSM 34978 and DSM 34674 produced protease activity that has the potential to compete with pure industrial enzymes. Simultaneously, the expression level of each activity was higher than of the respective expression level of prior art Bacillus velezensis strains which were already used in cleaning products. 25 I.4.2 Amylase Activities The results obtained in test series A, summarized in table 1-A, show the following: Likewise, as in case of the protease activity, the two Bacillus velezensis strains DSM 34978 and 30 DSM 34674 also proved to be very good in producing amylase activity. The tested supernatants, harvested from a 16 h cultivation, were found to contain amylases which degrade starch and produce a halo of degradation of the Ø sizes 7.54 mm and 7.34 mm for the strains DSM 34978 and DSM 34674, respectively. The corresponding α-amylase from Bacillus licheniformis with an activity of 250 mU was found to produce a halo of degradation of Ø 13.13 mm size. 35 The qualitative plate assay hence showed that the two Bacillus velezensis strains DSM 34978 and DSM 34674 produced amylase activity that can compete with pure industrial enzymes. Simultaneously, the expression level of each activity was well in the range of (and in case of DSM 34978 even higher than) the respective expression level of prior art Bacillus velezensis strains 1, 2, and 3, which were already 40 used in cleaning products (see table 1-A: Ø sizes of 7.50 mm, 5.99 mm, and 7.50 mm, respectively). As a202400143 Foreign Filings 93 further control, the amylase activity of two different species from the prior art was tested: Priestia megaterium DSM 33356 and Bacillus licheniformis DSM 13. Neither strain showed any amylase activity. The results obtained in test series B, summarized in table 1-B, show the following: 5 Bacillus velezensis strains DSM 34978 and DSM 34674 also showed remarkably high activity for amylase compared to the prior art Bacillus velezensis strain DSM 33857. As described under point I.2, the supernatants were harvested from a culture of each strain and adjusted to an optical density of OD 1 to standardize over growth effects. The degradation or clearance zones, measured as the diameter (“Ø”) in 10 mm, have a Ø size of 10.255 mm and 8.875 mm for DSM 34978 and DSM 34674, respectively. Bacillus velezensis strain DSM 33857 gave a Ø size of 10.13 mm, i.e. between the values of DSM 34978 and DSM 34674. Hence, Bacillus velezensis strains DSM 34978 showed the highest expression level of amylase compared to all other tested strains, including DSM 33857. I.4.3 Cellulase Activities 15 The cellulase activity was measured with a quantitative assay. The results obtained in test series A, summarized in table 1-A, show the following: 20 Just as in the case of the protease and amylase activity test, the supernatants of the two Bacillus velezensis strains DSM 34978 and DSM 34674 showed very high cellulase activity, which may be due to the fact that both strains were isolated from the soil containing different fiber and cellulose compounds which must be broken down to fuel their energy metabolism and keep them alive. 25 The normalized supernatant (OD 1) of Bacillus velezensis DSM 34978 showed an activity of 1660.76 mU, whereas the Bacillus velezensis DSM 34674 produced less cellulase, but overall displayed an activity of 1084.81 mU. These data were compared with the cellulase activity of Bacillus velezensis strains 1, 2, and 3 from product samples (see table 1-A: activity in mU / OD 1 of 944.01, 764.29, and 751.43, respectively). Not one of these comparative strains A to C could compete with the two high cellulase producers DSM 30 34978 and DSM 34674, as may be seen from table 1-A. Prior art Bacillus velezensis strain DSM 33857 showed an activity of 1340.49 mU, i.e. between the values of DSM 34978 and DSM 34674. Priestia megaterium DSM 33356 was tested in the same way and it was found that this strain did not display any cellulase activity. 35 I.4.4 Summary These data show that both strains Bacillus velezensis DSM 34978 and Bacillus velezensis DSM 34674 produce the highest concentrations of proteases and cellulases which are released in the environment to degrade several types of stains of organic origin and are better than already used strains of commercially202400143 Foreign Filings 94 available cleaning products. In addition, Bacillus velezensis strain DSM 34978 produces the highest concentration of amylases and cellulases, further improving its efficacy as microbial cleaning agent. II. Determination of protease activity of Priestia megaterium DSM 34980 5 Three different Priestia megaterium strains [DSM 34980, DSM 33356, and a commercially available Priestia megaterium strain (“strain 4”)] and one Bacillus velezensis strain [a commercially available Bacillus velezensis strain (“strain 5”)] were tested for protease activity in a testing procedure according to Assay A-II. The protease activity tested in Assay A-II is total protease activities, i.e. secreted protease activity as well as cell-bound protease activity. 10 Priestia megaterium DSM 34980 was isolated from soil rifled by wild boar. DSM 33356 is a prior art Priestia megaterium strain (WO 2021 / 129998 A1). The protease activity of each of these strains was assessed in two test series C and D. One further Priestia megaterium strain (abbreviated as “Priestia megaterium strain 4”) and one further 15 Bacillus velezensis strain (abbreviated as “Bacillus velezensis strain 5”) were isolated from commercially available cleaning products D and E, respectively, and investigated as comparisons. Strains of interest were grown separately on TSA-agar medium, overnight at 37 °C. Then, each strain was collected, washed three times with phosphate-buffered saline (“PBS”; Sigma, P4417-100TAB; 20 8000 x g centrifugation, 3 min, room temperature), and adjusted to an optical density (OD at λ = 600 nm) equal to 0.1. The test consists of applying 10 µl of the single strain suspensions onto skim milk media surfaces which mimic the food-like dirt that might be deposited on surfaces. For observing milk protease, skim milk agar medium (skim milk powder 28 g / L, casein enzymatic hydrolysate 5 g / L, yeast extract 2.5 g / L, glucose 1 g / L, agar 15 g / L) was used. The plates were incubated 25 for seven days at room temperature. Following the incubation, the respective protease enzymatic activity was indicated by a halo of degradation [diameter (“Ø”) in cm] surrounding active spots of growing bacteria. Two test series were performed. In the first test series C, the protease activity of Priestia megaterium 30 DSM 34980, Bacillus velezensis strain 5, and Priestia megaterium strain 4 was determined. The results are summarized in table 2-C. In the second test series D , the protease activity of Priestia megaterium strains DSM 34980 and DSM 33356 was determined. The results are summarized in table 2-D. 35 The results obtained in test series C are summarized in the following table 2-C: Table 3-C: Protease activities measured via a qualitative plate assay by determining the halo of degradation size (Ø in cm) which is visible of a grown colony on plate. The experiments were performed in two biological replicates and the means and standard deviations (“σ”) are given. Strain 4 and 5 were202400143 Foreign Filings 95 isolated from one commercially available cleaning product and are compared. DSM 34980 is a strain of Priestia megaterium. Strain Protease activity cells Ø halo of degradation [cm] 2.33 DSM 34980 (σ 0.1) 0.75 Strain 4 (Priestia megaterium) (σ 0.2) 1.8 Strain 5 (Bacillus velezensis) (σ 0.35) 5 The results obtained in test series D are summarized in the following table 2-D: Table 4-D: Protease activities measured via a qualitative plate assay by determining the halo of degradation size (Ø in cm) which is visible of a grown colony on plate. The experiments were performed 10 in two biological replicates and the means and standard deviations (“σ”) are given. DSM 34980 is a strain of Priestia megaterium. DSM 33356 is a prior art Priestia megaterium strain (disclosed in WO 2021 / 129998 A1). Strain Protease activity cells Ø halo of degradation [cm] 3.07 DSM 34980 (σ 0.1) 2.12 DSM 33356 (σ 0.15) The results obtained in test series C, summarized in table 2-C, show the following: 15 Surprisingly, Priestia megaterium DSM 34980 showed a halo of degradation of Ø size of 2.33 (± 0.1) cm. Another strain of the same species (strain 4), used in a commercially available cleaning product, showed a 1.58 cm smaller halo of degradation, i.e. of a Ø size of 0.75 (± 0.2) cm. A further comparative strain (strain 5) of the species Bacillus velezensis showed a better performance, however, still inferior to the 20 performance of Priestia megaterium strain DSM 34980 (table 2-C). The results obtained in test series D, summarized in table 2-D, show the following: In test series D, Priestia megaterium DSM 34980 showed a halo of degradation of Ø size of 3.07 (± 0.1) 25 cm. Priestia megaterium DSM 33356 showed a halo of degradation, i.e. of a Ø size of 2.12 (± 0.15) cm.202400143 Foreign Filings 96 Priestia megaterium strain DSM 34980 hence showed the most extended halo on skim milk protease plates. Thus, this strain sowed the highest degradation, indicating that during a long-term growth many milk proteases could be produced and were most likely at least in part cell-wall bound. 5 III. Determination of lipase activity of Bacillus subtilis DSM 34981 Three different Bacillus subtilis strains were tested for lipase activity in a testing procedure according to Assay G. 10 Bacillus subtilis DSM 34981 was isolated from an environmental soil sample. Two further Bacillus subtilis strains (abbreviated as “Bacillus subtilis strains 6 and 7”) were isolated from commercially available cleaning products D and B, respectively, and investigated as comparisons. In these tests, the ability to directly measure the hydrolysis of free p-NP due to a photometric assay was 15 used. The test was performed with 4 mmol / L 4-nitrophenyloctanoate (“4-NP-C8”; Sigma-Aldrich, CAS:1956-10-1). A stock solution S4NPC8 [confer step (G-3) supra] was prepared in iso-propanol and further diluted in 0.1 M Tris-buffer pH 8.5.20 µl of this stock solution of 4-NP-C8 was used in each test. For the preparation of the test solution, each bacterial strain of interest was pre-cultivated in 10 ml tryptic- 20 soy-broth [“TSB”; Merck- 105459; peptone from casein 17.0 g / L; peptone from soymeal 3.0 g / L; D(+) glucose monohydrate 2.5 g / L; sodium chloride 5.0 g / L; di-potassium hydrogen phosphate 2.5 g / L)) at 37 °C and 200 rpm overnight (16 h). A new main culture was inoculated with pre-culture to an OD at λ = 660 nm of 0.1. Beforehand the 25 pre-culture was washed twice with main culture medium MCM0(described in the context of Assay J). The main culture was incubated at 37 °C and 200 rpm agitation for 4 hours. Afterwards, the culture was harvested by centrifugation (5000 x g, 3 min, room temperature) and adjusted to OD 0.25 in 180 µl 0.1 M Tris-buffer.180 µl bacterial cell suspension was mixed with 20 µl 4-NP-C8 substrate solution S4NPC8(the preparation of S4NPC8is described in step (G-3) of Assay G) in a 96-well microliter plate 30 (Greiner bio one, Ref.655101) and incubated at 25 °C for 60 min in a Tecan spark plate reader. The determination was carried out in the Tecan plate reader at λ = 410 nm. Every 2 min, a measurement was done and after 60 min the final absorbance at λ = 410 nm was used for the evaluation. For the determination of the baseline, 20 µl substrate solution S4NPC8was mixed with 180 µl Tris buffer and as positive control different concentrations of a pure lipase from Candida rugosa (Sigma-Aldrich, L174) were 35 used. Additionally, a p-nitrophenol standard series (0-10 mmol / L) was prepared and used to quantify the amount of released p-NP (yellow) to determine the lipase activity in the different Bacillus suspensions. The activity of expressed lipase is given in mU / ml as mean value from two independent biological experiments. The results are summarized in table 3:202400143 Foreign Filings 97 Table 5: Lipase activities in mU / ml or in mU / OD 1 are shown as mean values (“σ”=standard deviation) of two biological replicates. For the quantification of lipase activity, the para-nitrophenyl (p-NP) ester with a C8 chain was used. The quantification was made based on a p-NP standard curve. Strains 6 and 7 from products D and B, respectively, belong to the Bacillus species subtilis as known for the DSM 34981. Strain Lipase activity mU / ml mU / OD1 DSM 34981 3.40 (σ 0.97) 2.72 (σ 0.77) Strain 6, product D 0.753 (σ 0.06) 0.60 (σ 0.04) Strain 7, product B 3.07 (σ 0.20) 2.46 (σ 0.16) 5 Surprisingly, Bacillus subtilis DSM 34981 showed the highest lipase production. The strain was isolated from an environmental soil sample and could hydrolyze 4-nitrophenyloctanonate into the C8-chain and p-nitrophenol. Already after 30 min, almost all of the 4 mM substrate was degraded and after 60 min the 10 activity was measured with 3.40 mU / ml which is comparable to the activity of 5µg / ml lipase from Candida rugosa. Tested strains 6 and 7 from commercially available cleaning products show an even lower activity tested for the same substrate (table 3). Bacillus subtilis DSM 34981 is hence an excellent candidate for degrading oil and grease indeed. The 15 responsible lipases are cell-wall bound or could be produced during the 1-hour of incubation with the substrate. IV. Determination of valeric acid metabolism IV.1 Determination of tolerance to valeric acid and the ability to metabolize valeric acid 20 Different Bacillus and Priestia species were tested for their ability to grow on valeric acid medium and their ability to metabolize valeric acid. For these investigations, a testing procedure according to Assay J was used. The tested Bacillus velezensis strains were Bacillus velezensis DSM 34978 and Bacillus velezensis DSM 34674. 25 The tested Bacillus licheniformis strains were Bacillus licheniformis DSM 34977 and prior art Bacillus licheniformis strain DSM 13 (disclosed in B. Veith et al., J Mol Microbiol Biotechnol 2004, 7, 204-211). The tested Priestia megaterium strain was Priestia megaterium DSM 34980. The tested Bacillus subtilis strain was Bacillus subtilis DSM 34981. 30 The ability to grow on valeric acid medium and the ability to metabolize valeric acid of each of these strains was assessed in two test series E and F. These six Bacillus / Priestia strains were tested in the presence of valeric acid (“VA”) in a “malodor control test”. In particular, in the malodor control test, it was tested whether these Bacillus / Priestia strains have202400143 Foreign Filings 98 the ability to tolerate and likewise to reduce 1000 ppm valeric acid. To this aim, the growth in a minimal medium with 1 wt.-% glucose as opposed to the growth in 1 wt.-% glucose with 0.1 wt.-% VA was compared. 5 Each Bacillus / Priestia strain of interest was pre-cultivated in 10 ml tryptic-soy-broth [“TSB”; Merck- 105459; peptone from casein 17.0 g / L; peptone from soymeal 3.0 g / L; D(+) glucose monohydrate 2.5 g / L; sodium chloride 5.0 g / L; di-potassium hydrogen phosphate 2.5 g / L] at 30 °C and 200 rpm overnight (16 h). The cells were washed with NaCl solution and used for inoculating the main culture. 10 For the main cultures, MCM+Valmedium as described in the context of Assay J and MCM0as described in the context of Assay J were used as media. For the cultivation of different Bacillus / Priestia strains inoculated in different media compositions a small cultivation system, Woulter-Deutz, was used, which allowed to measure up to 24 batches in parallel. 15 Main cultures were inoculated with washed pre-culture to OD 0.1 and were incubated at 30 °C with 225 rpm for 48 hours. After 48 hours, the final optical density at λ = 660 nm was measured of each culture and subsequently the supernatants were harvested by centrifugation (13000 x g, 3 min, room temperature). The concentration of valeric acid in the samples was quantified using an analysis method (see point VI.5.1.5). The values were compared to the medium control without a Bacillus / Priestia 20 inoculum. The percentage reduction of valeric acid based on the medium control was calculated for each batch with Bacillus / Priestia inoculum. Values were given as means of technical replicates. The quantification of valeric acid was done by the following analysis method. 25 All samples and a series of calibration standards were mixed with an internal standard (2-methylhexanoic acid). An excess of NaCl was added and samples were diluted with 1 part 50 wt.-% sulfuric acid to 4 parts sample. The resulting mixture was extracted in a ratio of 1 part diethyl ether to 1.25 parts sample for 10 minutes and then centrifuged for 10 minutes at 3000 x g. The organic supernatant was removed and, if necessary, further diluted to a concentration of 1 g / L. Samples and calibration standards were measured 30 using an Agilent GC 8860 equipped with split / spitless injector and FID detector on a GC column (BP21 30m; ID 0.32 mm; film 0.25 μm) at a flow rate of 1 ml / min He. The separation was carried out by means of a temperature gradient from 130 °C to 180 °C within 8.5 min. The chromatograms were evaluated by means of a multi-point area evaluation linear without zero crossing with 2-methylhexanoic acid as the internal standard. Valeric acid was eluting at 5.4 min within the program. 35 Two test series were performed. In the first test series E, the ability to grow on valeric acid medium and the ability to metabolize valeric acid of the following strains was determined: Bacillus velezensis DSM 34978 and Bacillus velezensis DSM 34674, Priestia megaterium DSM 34980, Bacillus licheniformis DSM 34977, and Bacillus subtilis DSM 34981. The results are summarized in table 4-E.202400143 Foreign Filings 99 The second test series F is a repetition of the first test series E, wherein a further prior art Bacillus velezensis strain DSM 13 (disclosed in B. Veith et al., J Mol Microbiol Biotechnol 2004, 7, 204-211) was tested. The results are summarized in table 4-F. 5 IV.2 Results The optical density at λ = 660 nm (OD) of cultures without and with VA after 48 h was measured. In addition, the reduction of VA of cultures with VA was determined. The results obtained in test series E are summarized in Table 4-E. 10 Table 6-E: Malodor reduction. The final OD at λ = 660 nm was measured of batches with and without VA after 48 h. Means are given. Delta OD was calculated based of final OD with VA to final OD without VA (“+” =increase, “- “= decrease). The VA in the different batches was quantified in the supernatant and given as percentage reduction compared to the start concentration / medium without bacterial inoculation. OD after 48 h OD after 48 h Delta OD compared VA reduction Strain w / o VA with VA to w / o VA after 48 h in % DSM 34978 0.986 0.626 -0.359 57 (B. velezensis) DSM 34977 0.377 1.662 +1.285 23 (B. licheniformis) DSM 34674 0.926 0.472 -0.454 41 (B. velezensis) DSM 34980 0.992 1.058 +0.065 29 (P. megaterium) DSM 34981 0.719 1.329 +0.610 8 (B. subtilis) 15 The results obtained in test series F are summarized in Table 4-F. Table 7-F: Malodor reduction. The final OD at λ = 660 nm was measured of batches with and without VA 20OD after 48 h OD after 48 h Delta OD compared VA reduction Strain w / o VA with VA to w / o VA after 48 h in % DSM 34978 1.234 0.957 -0.277 51 (B. velezensis) DSM 13 0.872 0.067 -0.805 9 (B. licheniformis)202400143 Foreign Filings 100 OD after 48 h OD after 48 h Delta OD compared VA reduction Strain w / o VA with VA to w / o VA after 48 h in % DSM 34977 0.853 2.490 +1.637 18 (B. licheniformis) DSM 34674 1.023 0.665 -0.358 59 (B. velezensis) DSM 34980 1.423 2.173 +0.750 37 (P. megaterium) DSM 34981 0.612 0.685 +0.073 11 (B. subtilis) From the results summarized in tables 4-E and 4-F, it follows that only three of the five strain samples, 5 namely the samples containing strains of Priestia megaterium (DSM 34980), Bacillus subtilis (DSM 34981), Bacillus licheniformis (DSM 34977), showed not only tolerance to grow in presence of VA, but, in fact, improved growth in the presence of VA. In addition, they showed the ability to metabolize and therefore to reduce VA from the culture medium. In particular, the following observations were made: 10 - Bacillus licheniformis DSM 34977, Priestia megaterium DSM 34980, and Bacillus subtilis DSM 34981 showed higher OD in presence of VA compared to the culture without VA. In particular, Bacillus licheniformis DSM 34977 showed the best performance when taking into account the VA reduction (23 % and 18 % reduction of VA from the culture medium in test series E and F, respectively) and the generation of biomass (Δ OD = +1.285 and +1.673 in test series E 15 and F, respectively). Such accumulation of biomass in presence of VA, combined with the VA metabolization rate that was observed for DSM 34977 is beneficial for the reduction of VA over time and helps to reduce odor-causing compounds in a long-lasting manner. Such combination of advantageous properties (high degradation rate of valeric acid and high growth of biomass) makes Bacillus licheniformis DSM 34977 an efficient VA (and hence, malodor) removal agent 20 with a long-lasting effect. This observation is even more surprising in view of the observations made for prior art Bacillus licheniformis strain DSM 13. This prior art strain does not accumulate biomass in the presence of VA: as shown in table 4-F, DSM 13 showed a reduction in biomass (Δ OD = -0.805), and in 25 addition, showed the lowest reduction of VA (only 9 % after 48 hours). - In case of Priestia megaterium DSM 34980, similar observations as for Bacillus licheniformis DSM 34977 were made: Priestia megaterium DSM 34980 showed a production of biomass which was slightly increased in the presence of VA (Δ OD = +0.065 and +0.750 in test series E and F, 30 respectively), but showed a rate of metabolization and thus reduction of VA from the culture medium that was even higher (29 % and 37 % in test series E and F, respectively) than the202400143 Foreign Filings 101 respective rate observed for Bacillus licheniformis DSM 34977. This points to the fact that this strain does not need VA for its metabolism, but the combination of these two observed features (slightly increased production of biomass with a high VA metabolization rate) also predestines this species as efficient VA (and hence, malodor) removal agent with a long-lasting effect. Both 5 strains exhibit exceptional characteristics in reducing the odor-causing compound VA, which is the result of the combination of two advantageous properties, i.e. the production of biomass and VA reduction. That is why both strains can be used efficiently for VA-caused malodor reduction with long-lasting effect; - Finally, Bacillus subtilis DSM 34981 also showed an accumulation of biomass during the 10 incubation over 48 hours (Δ OD = +0.610 and +0.073 in test series E and F, respectively). The VA reduction over 48 hours was only 8 % and 11 % in test series E and F, respectively. The combination of these two properties also predestines Bacillus subtilis DSM 34981 for VA-caused malodor reduction with long-lasting effect. 15 In summary, ΕXJ; 1000 ppm for each strain with ΓXJ; 1000 ppm > 1 may be determined as follows (given that the rate of metabolization of valeric acid medium kXJ; 1000 ppm is proportional to the measured VA reduction and thus may be equated in the following for simplicity): Test series E 20 - Bacillus licheniformis DSM 34977, kXJ; 1000 ppm~ 0.23; ΓXJ; 1000 ppm= 1.285 → ΕXJ; 1000 ppm= 0.29555; - Priestia megaterium DSM 34980, kXJ; 1000 ppm~ 0.29; ΓXJ; 1000 ppm= 0.065 → ΕXJ; 1000 ppm= 0.01885; - Bacillus subtilis DSM 34981, kXJ; 1000 ppm ~ 0.08; ΓXJ; 1000 ppm = 1.285 → ΕXJ; 1000 ppm = 0.1028. 25 Test series F - Bacillus licheniformis DSM 34977: kXJ; 1000 ppm ~ 0.18; ΓXJ; 1000 ppm = 1.637 → ΕXJ; 1000 ppm = 0.29466; - Priestia megaterium DSM 34980: kXJ; 1000 ppm ~ 0.37; ΓXJ; 1000 ppm = 0.750 → ΕXJ; 1000 ppm = 0.2775; - Bacillus subtilis DSM 34981: kXJ; 1000 ppm~ 0.11; ΓXJ; 1000 ppm= 0.073 → ΕXJ; 1000 ppm= 0.00803. 30 Mean value of Test series E and F - Bacillus licheniformis DSM 34977: ΕXJ; 1000 ppm= [0.29555 + 0.29466] / 2 = 0.295105; 35 - Priestia megaterium DSM 34980: ΕXJ; 1000 ppm = [0.2775 + 0.01885] / 2 = 0.148175; - Bacillus subtilis DSM 34981: ΕXJ; 1000 ppm = [0.1028 + 0.00803] / 2 = 0.055415. Hence, of all strains with ΓXJ; 1000 ppm> 1, Bacillus licheniformis DSM 34977 displayed the highest effectiveness ΕXJ; 1000 ppm to reduce valeric acid (1000 ppm). 40202400143 Foreign Filings 102 - On the other hand, Bacillus velezensis strains DSM 34978 (Δ OD = -0.359 and -0.277 in test series E and F, respectively) and DSM 34674 (Δ OD = -0.454and -0.358 in test series E and F, respectivel) showed a reduction in biomass over the course of the incubation period of 48 hours (ΓXJ; 1000 ppm < 1). Nevertheless, the VA reduction rate observed for these Bacillus velezensis 5 strains DSM 34978 (57 % and 51 % in test series E and F, respectively) and DSM 34674 (41 % and 59 % in test series E and F, respectively) was even higher than the respective rates observed for Bacillus licheniformis DSM 34977, Priestia megaterium DSM 34980, and Bacillus subtilis DSM 34981. Both Bacillus velezensis DSM 34978 and DSM 34674 strains were the most efficient strains to metabolize VA over the course of the incubation period, i.e. for 48 10 hours. However, as, they showed a decreased cell concentration after 48 hours in presence of VA, they demonstrated smaller tolerances for this organic acid. The high VA reduction rate, however, makes them predestined for use as a short-term agent for reduction of malodor that is caused by VA. 15 These observations demonstrate a long-term effect for malodor removal of the respective strains Priestia megaterium DSM 34980, Bacillus subtilis DSM 34981, Bacillus licheniformis DSM 34977. These strains l may be combined with the respective Bacillus velezensis strains DSM 34978 and DSM 34674 to give an effective agent for removal of malodor caused by valeric acid.202400143 Foreign Filings 103 Overview sequences* “yqcA” is not further characterized. “adaA” = methylphosphotriester-DNA-protein-cystein methyltransferase; “groEL” = chaperonin GroEL; 5 “gyrB” = DNA gyrase subunit B; “lipC” = spore germination lipase; “rpoB” = DNA-directed RNA polymerase subunit β; “uvrC” = excinuclease ABC subunit;202400143 Foreign Filings 104 “yqfD” = sporulation protein.

Claims

1. 202400143 Foreign Filings 105 Claims 1. A Priestia megaterium strain as deposited under DSM 34980 at the DSMZ and mutants thereof. 5 2. The Priestia megaterium strain according to Claims 1, wherein the mutant of Priestia megaterium DSM 34980 strain has protease activity, wherein, preferably, the protease activity is determined by the test according to Assay A-II.

3. The Priestia megaterium strain according to Claim 2, wherein the mutant of Priestia megaterium 10 DSM 34980 strain has a protease activity which is at least 93 %, more preferably at least 94 %, more preferably at least 95 %, more preferably at least 96 %, more preferably at least 97 %, more preferably at least 98 %, more preferably at least 99 %, more preferably at least 99.9 %, more preferably at least 99.99 %, more preferably at least 99.999 %, more preferably at least 100 % the protease activity of Priestia megaterium DSM 34980, and wherein, preferably, the protease activity of the mutant of Priestia 15 megaterium DSM 34980 relative to the protease activity of Priestia megaterium DSM 34980 is determined by the test according to Assay B-III.

4. The Priestia megaterium strain according to one of Claims 1 to 3, wherein the mutant of Priestia megaterium DSM 34980 strain exhibits at least one, preferably at least two, more preferably at least 20 three, even more preferably at least four, most preferably all five of the following characteristics i. to v.: i. a DNA sequence, which preferably is the DNA sequence coding for the 16S rRNA, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to 25 SEQ ID NO: 25; and / or ii. a DNA sequence, which preferably is a rpoB DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 26; and / or iii. a DNA sequence, which preferably is a gyrB DNA sequence, with a sequence identity of 30 at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 27; and / or iv. a DNA sequence, which preferably is a groEL DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO: 28; and / or 35 v. a DNA sequence, which preferably is a yqfD DNA sequence, with a sequence identity of at least 99 %, preferably at least 99.5 %, more preferably at least 99.9 %, even more preferably 100 %, to the polynucleotide sequence according to SEQ ID NO:

29.

5. The Priestia megaterium strain according to Claim 4, 40 wherein the mutant of Priestia megaterium DSM 34980 strain has a DNA sequence identity to the genomic DNA of strain DSM 34980 of at least 95 %.202400143 Foreign Filings 106 6. A preparation of Priestia megaterium DSM 34980 and / or a mutant thereof according to one of Claims 1 to 5. 5 7. A cleaning formulation F comprising Priestia megaterium DSM 34980 and / or a mutant of Priestia megaterium DSM 34980 according to one of Claims 1 to 5 or a preparation thereof according to Claim 6.

8. The cleaning formulation F according to Claim 7, which comprises at least one of surfactants,10 enzymes, builders, solvents, preservatives, benefit agents, polymers, bleaching systems, anti- redeposition aids, fibre protection agents, soil release agents, dye transfer inhibitors, fabric hueing agents, blueing dyes, enzyme stabilizing agents like boric acid, pH-regulators, emollients, emulsifiers, thickeners / viscosity regulators / stabilizers, UV photoprotective filters, antioxidants, hydrotropes, solids and fillers, film formers, pearlescent additives, deodorant and antiperspirant active ingredients, insect 15 repellents, self-tanning agents, preservatives, conditioners, perfumes, dyes, odour absorbers, cosmetic active ingredients, care additives, superfatting agents, solvents, malodor removers.

9. The cleaning formulation F according to Claim 7 or 8, further comprising at least one of the following: - Bacillus velezensis DSM 34674 strain and / or mutants thereof; 20 - Bacillus licheniformis DSM 34977 strain and / or mutants thereof; - Bacillus velezensis DSM 34978 strain and / or mutants thereof; - Bacillus subtilis DSM 34981 strain and / or mutants thereof.

10. A method of cleaning an object O or the human or animal body B comprising the following steps: 25 (a) contacting O or B with an, optionally diluted, cleaning formulation F according to one of Claims 7 to 9, wherein the Priestia megaterium DSM 34980 strain or a mutant thereof comprised by F is caused to produce protease activity before or while, preferably while, the, optionally diluted, cleaning formulation F is in contact with O or B, (b) separating at least a part of F from O or B, 30 (c) optionally rinsing O or B with further water.

11. The method according to Claim 10, wherein in step (a), the cleaning formulation F is diluted with water before or while, preferably while, the cleaning formulation F is in contact with O or B. 35 12. The method according to Claim 10 or 11, wherein an object O is cleaned, preferably at a temperature in step (a) in a range of from 10 °C to < 100 °C.

13. Use of the cleaning formulation F according to one of Claims 7 to 9 for cleaning an object O or the human or animal body B. 40202400143 Foreign Filings 107 14. A food or feed E comprising Priestia megaterium DSM 34980 and / or a mutant of Priestia megaterium DSM 34980 according to one of Claims 1 to 5 or a preparation thereof according to Claim 6.

15. A method of feeding animals, wherein the animals are fed with feed or food E according to Claim 14.

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