Apolipoproteins for use in cleaning compositions

Abstract

In the present invention, new components for cleaning compositions are provided. Particularly, the present invention provides apolipoproteins that can be used to improve cleaning compositions.

Description

Apolipoproteins for use in cleaning compositionsField of the inventionIn the present invention new components for cleaning compositions are provided. Particularly, the present invention provides apolipoproteins that can be used to improve cleaning compositions.Background of the inventionProteins, in particular enzymes, are increasingly used in various applications as sustainable alternatives to petrochemistry. Enzymes are biobased catalysts that can be for the degradation of various components. In particular, in the detergent industry, enzymes are therefore implemented in washing formulations to improve cleaning efficiency, to increase sustainability, and to reduce the amounts of surfactants and polymers in a washing step.For instance, proteases are frequently used to remove proteinaceous stains, amylases are very effective in removing starch-containing stains and lipases as well as cutinases can remove stains comprising fats and / or lipids. Despite this, enzymatic cleaning of stains, particularly complex stains, in particular stains comprising one or more selected from fats, oils, and lipids, like stains from sebum and make-up, as well as complex bleachable stains, likes stains from fruits, vegetables, tea, coffee, or ink, still remains a challenge. For instance, the enzymatic activity of lipases and other lipolytic enzymes on stains comprising fats and / or lipids result in short chain fatty acids that are the cause of malodor formation, which often remains with the washed and dried items.Sebum is a complex mixture of components produced by sebaceous glands in the skin, primarily composed of triglycerides, fatty acids, wax esters, squalene, and cholesterol, which serves to lubricate and protect the skin and hair. However, the nature of sebum presents significant challenges in cleaning applications, particularly in household and personal care products, where traditional detergents and cleaning agents often struggle to effectively remove these types of stains. The accumulation of sebum on fabrics, surfaces, and skin can lead to unsightly residues, odors, and degradation of materials, necessitating the development of more efficient cleaning solutions. Therefore, current methods also frequently rely on harsh chemical formulations or excessive scrubbing, which can damage delicate fabrics or irritate the skin, highlighting the need for innovative cleaning approaches that target the components of sebum without compromising the integrity of the substrates being cleaned and without causing malodorous side products.For standard detergents, also complex organic, pigmented stains, like stains from fruits, vegetables, tea, coffee, ink, or make-up, also remain a challenge. Traditionally, bleach has been used for tackling these types of stains. However, its use is often accompanied by several disadvantages, including fabric damage, color fading, and the release of harmful byproducts during application.Lipopeptides, like surfactin, are amphiphilic compounds comprising a short, circular chain of amino acids and a lipophilic side chain. Due to their amphiphilic nature lipopeptides were considered as putative surfactants for detergents (e.g., DE102012220103). However, lipopeptides have a strong tendency to interact with mammaliancell membranes and to cause lysis of mammalian cells, making lipopeptides not well-suited for a safe use in detergents.The present inventors surprisingly revealed that amphiphilic proteins comprising a chain of amino acids longer than in lipopeptides (called as apolipoproteins) are effective in cleaning complex stains for example coming from sebum, fruits, vegetables, coffee, ink, or make-up, without causing malodorous side products derived from enzymatic degradation. Thus, apolipoproteins can be used in detergents in addition to, but also as an alternative to surfactants as well as polymers and certain types of enzymes.Brief summary of the inventionThus, the present invention is directed to the use of apolipoproteins in cleaning compositions, the apolipoproteins and compositions comprising these apolipoproteins. Additionally, methods for removing stains using a composition comprising such apolipoproteins are provided.Detailed description of the inventionThe present invention may be understood more readily by reference to the following detailed description of the embodiments of the invention and the examples included herein.Although the present invention will be described with respect to particular embodiments, this description is not to be construed in a limiting sense.DefinitionsUnless otherwise noted, the terms used herein are to be understood according to conventional usage by those of ordinary skill in the relevant art.Before describing in detail exemplary embodiments of the present invention, definitions important for understanding the present invention are given. Unless stated otherwise or apparent from the nature of the definition, the definitions apply to all compounds, methods and uses described herein.As used in this specification and in the appended claims, the singular forms of "a" and "an" also include the respective plurals unless the context clearly dictates otherwise.In the context of the present invention, the terms "about" and "approximately" denote an interval of accuracy that a person skilled in the art will understand to still ensure the technical effect of the feature in question. The term typically indicates a deviation from the indicated numerical value of ±20 %, preferably ±15 %, more preferably ±10 %, and even more preferably ±5 %.Furthermore, the terms "first", "second", "third" or "(a)", "(b)", "(c)", "(d)" etc. and the like in the description and in the claims, are used for distinguishing between similar elements and not necessarily for describing a sequential or chronological order. It is to be understood that the terms so used are interchangeable under appropriate circumstances and that the embodiments of the invention described herein are capable of operation in other sequences than described or illustrated herein. In case the terms "first", "second", "third" or "(a)", "(b)", "(c)", "(d)", "i", "ii" etc. relate to steps of a method or use or assay there is no time or time interval coherence between the steps, i.e. the steps may be carried out simultaneously or there may be time intervals of seconds, minutes, hours,days, weeks, months or even years between such steps, unless otherwise indicated in the application as set forth herein above or below.Throughout this application, various publications are referenced. The disclosure of all these publications and those references cited within those publications in their entireties are hereby incorporated by reference into this application in order to more fully describe the state of the art to which this invention pertains.It is to be understood that the term "comprising" is not limiting. For the purposes of the present invention the term "consisting of" is considered to be a preferred embodiment of the term "comprising". If hereinafter a group is defined to comprise at least a certain number of members, this is meant to also encompass a group which consists of these members only."Amino acid substitutions” are described by providing the original amino acid followed by the number of the position within the amino acid sequence, followed by the substituted amino acid. For example, the substitution of histidine at position 120 with alanine is designated as"His120Ala” or"H120A”. Substitutions can also be described by merely naming the resulting amino acid in the variant without specifying the amino acid of the parent at this position, e.g., by using "X120A” or "120A” or "Xaa120Ala” or “120Ala” .Variants comprising multiple substitutions are separated by "+”, e.g., "Arg170Tyr+Gly 195Glu”, "R170Y+G195E” or "X170Y+X195E” representing a substitution of arginine and glycine at positions 170 and 195 with tyrosine and glutamic acid, respectively. Alternatively, multiple substitutions may be separated by space or a comma, e.g., "R170Y G195E” or "R170Y, G195E” respectively. Where different alternative substitutions can be introduced at a position, the different substitutions are separated by a comma, e.g., “Arg170Tyr,Glu” and "R170T, E”, respectively, represents a substitution of arginine at position 170 with tyrosine or glutamic acid. Alternative substitutions at a particular position can also be indicated as "X120A,G,H”, “120A,G,H", "X120A / G / H”, or “120A / G / H”. Alternatively, different substitutions may be indicated in brackets, e.g., "Arg 170[Tyr, Gly]” or "Arg 170{Tyr, Gly}” or in short "R170 [Y,G]” or “R170 {Y,G}”.The term "native” (or "naturally” or "wild-type” or "endogenous”) cell or organism or polynucleotide or polypeptide refers to the cell or organism or polynucleotide or polypeptide as found in nature (i.e., without there being any human intervention).The term "heterologous” (or "exogenous” or "foreign” or "recombinant” or "non-native” or "non-natural”) polypeptide is defined herein as a polypeptide that is not native to the host cell, a polypeptide native to the host cell in which structural modifications, e.g., deletions, substitutions, additions, and / or insertions, have been made by recombinant DNA techniques to alter the native polypeptide, or a polypeptide native to the host cell whose expression is quantitatively altered or whose expression is directed from a genomic location different from the native host cell as a result of manipulation of the DNA of the host cell by recombinant DNA techniques, e.g., a stronger promoter. Similarly, the term "heterologous” (or "exogenous” or "foreign” or "recombinant” or "non-native” or "non-natural”) polynucleotide refers to a polynucleotide that is not native to the host cell, a polynucleotide native to the host cell in which structural modifications, e.g., deletions, substitutions, additions, and / or insertions, have been made by recombinant DNA techniques to alter the native polynucleotide, or a polynucleotide native to the host cell whose expression is quantitatively altered as a result of manipulation of the regulatory elements of the polynucleotide byrecombinant DNA techniques, e.g., a stronger promoter, or a polynucleotide native to the host cell, but integrated not within its natural genetic environment as a result of genetic manipulation by recombinant DNA techniques. With respect to the relation between two or more polynucleotide sequences or the relation between two or more amino acid sequences, the term "heterologous” is used to characterize that the two or more polynucleotide sequences or two or more amino acid sequences are naturally not occurring in the specific combination with each other.For the purpose of the invention, "recombinant" (or "transgenic”) with regard to a cell or an organism means that the cell or organism contains a heterologous polynucleotide, which is introduced by people using gene technology. Regarding a polynucleotide, the term "recombinant” includes all constructs produced by using gene technology I recombinant DNA techniques in which either(a) the sequence of the polynucleotide or a part thereof, or(b) one or more genetic control sequences, which are operably linked to the polynucleotide, including but not limited to a promoter, or(c) both a) and b) are not located in their wild-type genetic environment or have been modified by people.A "synthetic" compound is obtained by in vitro chemical and / or enzymatic synthesis.Variant polynucleotide and variant polypeptide sequences may be defined by their sequence identity when compared to a parent sequence.Sequence identity usually is provided as "% sequence identity” or "% identity”. For calculation of sequence identities, in the first step a sequence alignment is produced. According to this invention, a pairwise global alignment is produced, meaning that two sequences are aligned over their complete length, which is usually produced by using a mathematical approach, called alignment algorithm.According to the invention, the alignment is generated by using the algorithm of Needleman and Wunsch (J. Mol. Biol. (1970) 48, p. 443-453). Preferably, the program "NEEDLE” (The European Molecular Biology Open Software Suite (EMBOSS)) is used for the purposes of the current invention, with using the programs default parameter (polynucleotides: gap open=10.0, gap extend=0.5 and matrix=EDNAFULL; polypeptides: gap open=10.0, gap extend=0.5 and matrix=EBLOSUM62). After aligning two sequences, in a second step, an identity value is determined from the alignment produced. For this purpose, the %-identity is calculated by dividing the number of identical residues by the length of the alignment region which is showing the respective sequence of the present invention over its complete length multiplied with 100: %-identity = (identical residues I length of the alignment region which is showing the respective sequence of the present invention over its complete length) *100.A special aspect concerning amino acid substitutions are "conservative mutations”, interchangeably used with "conservative substitutions” herein. Conservative mutations are those where one amino acid is exchanged with a similar amino acid. Herein the following conservative exchanges are considered: Amino acid A is similar to amino acids S, Amino acid D is similar to amino acids E; N, Amino acid E is similar to amino acids D; K; Q, Amino acid F is similar to amino acids W; Y, Amino acid H is similar to amino acids N; Y, Amino acid I is similar to amino acids L; M; V, Amino acid K is similar to amino acids E; Q; R, Amino acid L is similar to amino acids I; M; V, Amino acid M is similar to amino acids I; L; V, Amino acid N is similar to amino acids D; H; S, Amino acid Q is similar toamino acids E; K; R, Amino acid R is similar to amino acids K; Q, Amino acid S is similar to amino acids A; N; T, Amino acid T is similar to amino acids S, Amino acid V is similar to amino acids I; L; M, Amino acid W is similar to amino acids F; Y, and Amino acid Y is similar to amino acids F; H; W.A "fragment" or "subsequence” as used herein refers to a portion of an amino acid sequence. The fragment comprises consecutive amino acids compared to the original full length amino acid sequence, respectively. Polypeptides comprising a deletion of one or more amino acids at the N terminus and / or the C terminus of the polypeptide and essentially retain the activity of the protein are herein designated as "functional fragments". Preferably, the functional fragment has at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80% identical, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 98.5 %, at least 99%, or at least 99.5% of the length of the original full length amino acid sequence. Preferably, the functional fragment comprises 100 to 350 or 100 to 200 consecutive amino acids of the full-length polypeptide. Also preferably, the functional fragment retains at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80% identical, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 98.5 %, at least 99%, at least 99.5% or at least 100% of the activity of the original full length amino acid sequence. In the context of the present invention, the "original full length amino acid sequence" is an amino acid sequence which is at least 60% identical to the amino acid sequence according to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6 and which has the same length as the amino acid sequence according to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, respectively.In one embodiment, the apolipoprotein of the present invention does not comprise any internal deletions compared to the amino acid sequence according to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6. The apolipoprotein of the present invention may comprise a deletion of one or more amino acids at the N terminus and / or the C terminus of the apolipoprotein."Genetic construct” or "nucleic acid construct” or "expression cassette” as used herein, is a nucleic acid molecule composed of at least one sequence of interest to be expressed, operably linked to one or more control sequences (at least to a promoter) as described herein.The term "vector” as used herein comprises any kind of construct suitable to carry foreign polynucleotide sequences for transfer to another cell, or for stable or transient expression within a given cell. The term "vector” as used herein encompasses any kind of cloning vehicles, such as but not limited to plasmids, phagemids, viral vectors (e.g., phages), bacteriophage, baculoviruses, cosmids, fosmids, artificial chromosomes, and any other vectors specific for specific hosts of interest. Foreign polynucleotide sequences usually comprise a coding sequence which may be referred to herein as "gene of interest”. The gene of interest may comprise introns and exons, depending on the kind of origin or destination of host cell.The term "introduction of a polynucleotide” or "transformation of a polynucleotide” as referred to herein encompasses the transfer of an exogenous polynucleotide into a host cell, irrespective of the method used for transfer. That is, the term "transformation of a polynucleotide” as used herein is independent from vector, shuttle system, or host cell, and it not only relates to the polynucleotide transfer method of transformation as known in the art (of., for example, Sambrook, J. et al. (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY), but it encompasses any further kind of polynucleotide transfer methods such as, but not limited to, transduction or transfection.A polynucleotide encoding a polypeptide may be "expressed”. The term "expression” or "gene expression” means the transcription of a specific gene or specific genes or specific nucleic acid construct. The term "expression” or "gene expression” means the transcription of a gene or genes or genetic construct into structural RNA (e.g., rRNA, tRNA) or mRNA with or without subsequent translation of the latter into a protein. The process includes transcription of DNA and processing of the resulting mRNA product.The term "purification” or "purifying” (or "isolation” or "isolating”) refers to a process in which at least one component, e.g., a protein of interest, is separated from at least another component, e.g., a particulate matter of a fermentation broth, and transferred into a different compartment or phase, wherein the different compartments or phases do not necessarily need to be separated by a physical barrier. Examples of such different compartments are two compartments separated by a filtration membrane or cloth, i.e., filtrate and retentate; examples of such different phases are pellet and supernatant or cake and filtrate, respectively. The resulting solution after purifying the protein of interest is called herein "purified protein solution”."Protein formulation” (or "polypeptide formulation”), e.g., "apolipoprotein formulation”, means any non-complex formulation comprising a small number of ingredients, preferably, 2-8 components, wherein the ingredients serve the purpose of stabilizing the protein comprised in the protein formulation and / or the stabilization of the protein formulation itself. Preferably, the non-complex protein formulation comprises the protein in higher concentrations than the complex formulation, e.g., than a detergent formulation. Thus, preferably the non-complex protein formulation is a concentrated protein formulation. Preferably, non-complex protein formulations comprise 20 to 120 mg / g protein, whereas complex formulations, like cleaning compositions, comprise 0.002 to 10 mg / g protein. In contrast to a non-complex formulation, a complex formulation means herein a formulation comprising a higher number of ingredients, preferably, 9-30 components, wherein the ingredients serve the purpose of stabilizing the proteins comprised in the protein formulation and / or the stabilization of the protein formulation itself, but additionally the complex formulation comprises components that serve the purpose of the complex formulation, e.g., a cleaning composition. An example for a non-complex protein formulation is a concentrated protein composition that is used as a stock-solution to prepare a complex formulation, e.g., a cleaning composition, wherein in the cleaning compositions other compounds are present that serve the cleaning purpose of the cleaning composition, e.g., surfactants and / or chelating agents.The term "protein stability” according to the current invention relates to the retention of protein activity as a function of time during storage or operation. Retention of protein activity as a function of time during storage is called "storage stability”.To determine and quantify changes in the activity of proteins stored or used under certain conditions over time, the activity is measured under defined conditions at time zero (100%) and at a certain point in time later (x%). By comparison of the values measured, the residual activity of the protein can be determined in its extent. The extent of the residual activity of the protein determines a protein's stability or non-stability.The term "detergent stability” (also called herein "residual activity in a detergent” or "storage stability in a detergent composition”) refers to the ability of a protein to exert activity (in the case of the protein being an enzyme, "detergent stability” refers to the ability of the enzyme to exert enzyme activity), preferably measured as wash performance, after storage in a detergent composition, preferably, at a temperature of 22 °C, 37 °C, 45 °C, or 50 °C for up to 14 days in a detergent composition (preferably, in an ES1-C formulation as described herein). Most preferably, "detergent stability” is determined by measuring wash performance of the protein after storage at a temperature of 22 °C for 18 hours in a detergent composition (preferably, in an ES1-C formulation as described herein).As used herein, "wash performance" (also called herein "cleaning performance”) of a protein refers to the contribution of the protein to the cleaning performance of a cleaning composition, i.e. the cleaning performance added to the cleaning composition by the performance of the protein. The term "wash performance” is used herein similarly for laundry and hard surface cleaning. Wash performance is compared under relevant washing conditions. The term "relevant washing conditions" is used herein to indicate the conditions, particularly washing temperature, time, washing mechanics, sud concentration, type of detergent and water hardness, actually used in households in a detergent market segment. The term "improved wash performance", "improved cleaning", "improved stain removal", "improved brightness", "increased whiteness", or "brightening" is used to indicate that a better end result is obtained in stain removal under relevant washing conditions relative to the corresponding control condition, wherein the corresponding control condition is preferably the use of no apolipoprotein of the present invention, e.g., detergent alone without the apolipoprotein of the present invention.As used herein, the term "specific performance" refers to the cleaning and removal of specific stains or soils per unit of active protein. In one embodiment, the specific performance is determined using stains comprising one or more selected from fats, oils, and lipids, such as sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, or lipstick.The term "detergent composition” or "cleaning composition" (also called "cleaning formulation”, "detergent formulation” or "detergent” herein), as used herein, refers to compositions and formulations designed for cleaning soiled material. Cleaning compositions include those designed for cleaning soiled material or surfaces of any kind. Cleaning compositions are complex formulations as further defined herein. Cleaning compositions include cleaning compositions for different applications such as laundry and hard surface cleaning. Cleaning compositions also include biodegradable cleaning compositions. The term "detergent component” or "cleaning component” (also called herein as "adjunct cleaning additive”) is defined herein to mean a type of chemical, which can be used in detergent compositions. A typical detergent component is a surfactant. "Surfactant" (synonymously used herein with "surface active agent”) means an organic chemical that, when added to a liquid, changes the properties of that liquid at an interface. According to its ionic charge, a surfactant is called non-ionic, anionic, cationic, or amphoteric. The term "effective amount of a detergent component” includes amounts of certain components to provide effectivestain removal and / or effective cleaning conditions (e.g. pH, temperature, water hardness, quantity of foaming), amounts of certain components to effectively provide optical benefits (e.g. optical brightening, dye transfer inhibition, color care), and amounts of certain components to effectively aid the processing (maintain physical characteristics during processing, storage and use; e.g. rheology modifiers, hydrotropes, desiccants).The term "laundry” or "laundering” relates to both household laundering and industrial laundering and means the process of treating textiles and / or fabrics with a solution containing a detergent composition. The laundering process may be carried out by using technical devices such as a household or an industrial washing machine. Alternatively, the laundering process may be done by hand.The term "textile” means any textile material including yarns (thread made of natural or synthetic fibers used for knitting or weaving), yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, as well as fabrics made of these materials such as garments, cloths and other articles. The terms "fabric” refers to a textile made by weaving, knitting or felting fibers and the term "garment” refers to any kind of article of clothing made of textile.The term "fibers” includes natural fibers, synthetic fibers, and mixtures thereof. Examples of natural fibers are of plant (such as flax, jute and cotton) or animal origin, comprising proteins like collagen, keratin and fibroin (e.g. silk, sheep's wool, angora, mohair, cashmere). Examples for fibers of synthetic origin are polyurethane fibers such as Spandex® or Lycra®, polyester fibers, polyolefins such as elastofin, or polyamide fibers such as nylon. Fibers may be single fibers or parts of textiles such as knitwear, woven or non-woven fabrics.The term "hard surface cleaning” relates to both household hard surface cleaning and industrial hard surface cleaning and means the process of treating hard surfaces with a solution containing a detergent composition. Hard surfaces may include any hard surfaces in the household or industry, such as floors, furnishing, walls, sanitary ceramics, glass, metallic surfaces including cutlery or dishes and medical devices such as diagnostic instruments, trays, pans, holders, racks, forceps, scissors, shears, saws (e.g. bone saws and their blades), hemostats, knives, chisels, rongeurs, files, nippers, drills, drill bits, rasps, burrs, spreaders, breakers, elevators, clamps, needle holders, carriers, clips, hooks, gouges, curettes, retractors, straightener, punches, extractors, scoops, keratomes, spatulas, expressors, trocars, dilators, cages, glassware, tubing, catheters, cannulas, plugs, stents, endoscopes, arthoscopes and related equipment. A particular form of hard surface cleaning is dishwashing, particularly automatic dishwashing (ADW).The term "dish wash” refers to all forms of washing dishes, e.g. by hand or automatic dish wash. Washing dishes includes, but is not limited to, the cleaning of all forms of crockery such as plates, cups, glasses, bowls, all forms of cutlery such as spoons, knives, forks and serving utensils as well as ceramics, plastics such as melamine, metals, china, glass and acrylics.In the field of detergency, usually the term "stains” is used with reference to laundry, e.g., cleaning of textiles, fabric, or fibers, whereas the term "soils” is usually used with reference to hard surface cleaning, e.g., cleaning of dishes and cutlery. However, herein the terms "stain” and "soil” shall be used interchangeably...Complex stains" are defined as multi-component stains that consist of a heterogeneous mixture of various substances, including but not limited to proteins, lipids, carbohydrates, and pigments, which can originate fromdiverse sources such as food products, biological fluids, and environmental contaminants. These stains exhibit intricate interactions among their constituent materials, making them more challenging to remove than singlecomponent stains. Examples of complex stains include, but are are not limited to, sebum and bleachable stains, like stains coming from fruits, vegetables, tea, coffee, ink, or make-up.„Bleachable stains" are discolorations on fabrics or surfaces that can be effectively removed or lightened through the use of bleaching agents (like sodium hypochlorite or hydrogen peroxide), typically because they contain chromophores, that are susceptible to oxidation or degradation by these agents. These stains often arise from organic materials, such as food, beverages, fruits, vegetables, tea, coffee, ink or make-up, and can vary in intensity and composition.A composition "essentially devoid” of a compound shall mean herein that the respective compound is not added to the composition on purpose, meaning that at most non-effective amounts are present, most preferably 0% of the compound are contained in the composition.A "composition” is a mixture of components (also called ingredients) prepared according to a specific formula. Compositions can be liquid or solid. Liquid compositions of the invention include solutions, emulsions and dispersions, gels etc. as long as the liquid is fluid and pourable. Liquid compositions according to the present invention preferably have a dynamic viscosity in the range of about 500 to about 20,000 mPa*s, determined at 25°C according to Brookfield, for example spindle 3 at 20 rpm with a Brookfield viscosimeter LVT-II."Gel", as used herein, means a shear thinning, lamellar gel, with a pouring viscosity in the range of from 100 to 5,000 mPa*s (milli Pascal seconds), more preferably less than 3,000 mPa*s, most preferably less than 1 ,500 mPa*s. Compositions include protein compositions, e.g. liquid protein compositions as described herein, and cleaning compositions, e.g. liquid cleaning compositions as described herein.The components of the composition can be separated by formulating them in different compartments, such as different compartments of multi-chamber-pouches or bottles having different chambers, from which the liquids are poured out at the same time in a predefined amount to assure the application of the right amount per individual point of use of each component from each chamber. Such multi-compartment-pouches and bottles etc. are known to a person of skill as well.Detailed descriptionIn the present invention new apolipoproteins are provided. Additionally, compositions comprising the apolipoproteins and methods of making and using the apolipoproteins are provided. In particular, the use of apolipoproteins for cleaning is provided.ApolipoproteinsApolipoproteins according to the invention are proteins characterized by specific amphiphilic properties that enable the proteins to interact effectively with lipophilic substances such as fats, lipids, and oils. Thus, these proteins on the one hand possess hydrophobic regions that facilitate binding to hydrophobic molecules, like fats, lipids, and oils, allowing it to bind, emulsify, and / or disperse these hydrophobic molecules, while on the otherhand also containing hydrophilic regions that promote solubility in aqueous environments. Without being bound by theory, by stabilizing oil-in-water emulsions and / or binding to fatty soil constituents, the apolipoprotein enhances the cleaning efficacy of detergent formulations, improving the removal of stains comprising one or more selected from fats, oils, and lipids, preferably complex stains, like sebum, from surfaces of an object, e.g., textile or hard surface. In contrast to lipopeptides, which usually comprise an amino acid chain of 2-25 amino acids, apolipoproteins do have a longer chain of amino acids, preferably 30-900, more preferably 50-800, more preferably 100-700, most preferably 100-500 amino acids. For this reason apolipoproteins can also be called “apolipopolypeptides” or “lipopolypeptides” . Herein, apolipoproteins may also be called ..lipoproteins". This is in particular due to them being lipid-like proteins. However, in order to underline that the proteins of the present invention represent the proteinaceous part of the lipid / protein-structures, which are formed as part of the cleaning process, and as the term "lipoprotein” is sometimes used for such lipid / protein-structures, the term "apolipoprotein” is preferably used herein. Apolipoproteins according to the present invention do not possess enzymatic activity. Preferably, apolipoproteins of the present invention are devoid of any lipid and / or fatty acid covalently bound to the amino acid sequence, preferably, apolipoproteins of the present invention consist of a chain of amino acids, preferably selected from more than one type of amino acid. Preferably, apolipoproteins of the present invention do not comprise post-translational modifications. Preferably, the amino acid chain of apolipoproteins of the present invention is not a circular amino acid chain. Preferably, the apolipoproteins of the present invention are of bacterial origin.Apolipoproteins can thus be used in cleaning compositions for the removal of stains, preferably complex stains. Apolipoproteins can thus be used in cleaning compositions for the removal of stains, preferably complex stains preferably stains comprising one or more selected from fats, oils, and lipids.Apolipoproteins can also be used in cleaning compositions for the removal of stains, preferably complex stains, preferably stains comprising one or more chromophores (color-causing molecules), preferably bleachable stains. Apolipoproteins can also be used in cleaning compositions for the removal of stains, preferably complex stains, preferably stains comprising one or more selected from fats, oils, and lipids and one or more chromophores (color-causing molecules), preferably bleachable stains.Apolipoproteins can thus be used in cleaning compositions for the removal of stains, preferably sebum and / or bleachable stains, like stains from tea, coffee, ink, make-up, grass, fruits, vegetables, nuts, legumes, raspberry, blueberry, cherry, redcurrant, blackcurrant, juices, ketchup, marmalade, wine, cocoa, or chocolate, preferably tannin-containig stains, like stains from wine, tea, or coffee, and / or anthocyanin-containing stains like stains from raspberry, blueberry, cherry, redcurrant, and blackcurrant, most preferably stains from tea or coffee.The effect of apolipoproteins can be measured by determining wash performance, removal of stains, brightening and / or increase in whiteness, for instance, as described herein in the examples.Wash performance, removal of stains, brightening and / or increase in whiteness can be measured using RGB (Red, Green, Blue) values by calculating various indices that quantify the wash performance, removal of stains, brightening and / or increase in whiteness of a surface. One common approach is to convert RGB values into a perceived brightness value using a formula that reflects human vision.Additionally, tools such as colorimeters can be used to measure these RGB values directly from surfaces, allowing for accurate assessments of performance, removal of stains, brightening and / or increase in whiteness in practical applications.Preferably, the apolipoprotein of the present invention displays detergent stability as described herein.Preferably, the apolipoprotein of the present invention is a purified, synthetic, and / or recombinant apolipoprotein. Preferably, the apolipoprotein of the present invention is a purified apolipoprotein.In one embodiment of the present invention, the apolipoprotein comprises a sugar binding domain.Preferably, the present invention refers to a protein that comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, wherein the protein is preferably an apolipoprotein.Preferably, the apolipoprotein of the present invention is an apolipoprotein that comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6.Preferably, the apolipoprotein of the present invention is an apolipoprotein that comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 6.Preferably, the apolipoprotein of the present invention is an apolipoprotein that comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 6, or at least 98% at least 99%, or 100% identical to SEQ ID NO: 4.Preferably, the apolipoprotein of the present invention is an apolipoprotein that comprises an amino acid sequence that is at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6.Preferably, the apolipoprotein of the present invention is an apolipoprotein that comprises an amino acid sequence that is at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 6.In one embodiment, the apolipoprotein of the present invention is an apolipoprotein that comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 4, wherein the apolipoprotein comprises one or more, preferably all,of the amino acids selected from the group consisting of K45, S46, S52, S56, N57, A58, 174, and Y108, according to the numbering of SEQ ID NO: 4.Preferably, the apolipoprotein of the present invention is an apolipoprotein that comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1 , SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1.In another embodiment, the apolipoprotein of the present invention is an apolipoprotein that comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 14, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, or SEQ ID NO: 13, preferably SEQ ID NO: 8, SEQ ID NO: 9, or SEQ ID NO: 14, preferably SEQ ID NO: 8 or SEQ ID NO: 9, preferably SEQ ID NO: 8.In one embodiment, the apolipoprotein comprises an amino acid sequence that is with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1 , preferably at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1 .In another embodiment, the apolipoprotein comprises an amino acid sequence that is with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 2, preferably at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 2.In another embodiment, the apolipoprotein comprises an amino acid sequence that is with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 3, preferably at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 3.In another embodiment, the apolipoprotein comprises an amino acid sequence that is with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 4, preferably at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 4.In another embodiment, the apolipoprotein comprises an amino acid sequence that is with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or100% identical to SEQ ID NO: 5, preferably at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 5.In another embodiment, the apolipoprotein comprises an amino acid sequence that is with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 6, preferably at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 6.In another embodiment, the apolipoprotein comprises an amino acid sequence that is with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 7, preferably at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 7.Most preferably, the apolipoprotein comprises an amino acid sequence that is with increasing preference at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identical to preferably SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1.In one embodiment, the apolipoprotein comprises or consists of an amino acid sequence that is 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1.In one embodiment, the apolipoprotein comprises or consists of an amino acid sequence that is 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1, but comprising 1-20, preferably 1-15, more preferably 1-10, or even more preferably 1-5 amino acid substitutions, preferably conservative amino acid substitutions.Ways of introducing amino acid alterations, e.g., substitutions, preferably conservative substitutions, into protein sequence are well known in the art. Substitutions can be introduced by using any mutagenesis procedure known in the art, such as site-directed mutagenesis, synthetic gene construction, semi-synthetic gene construction, random mutagenesis, shuffling, etc., followed by a relevant screening procedure. See, e.g., Scherer and Davis, 1979, Proc. Natl. Acad. Sci. USA 76: 4949-4955; and Barton et al., 1990, Nucleic Acids Res. 18: 7349-4966, U.S. Patent Application Publication No. 2004 / 0171154; Storici et al., 2001, Nature Biotechnol. 19: 773-776; Kren et al., 1998, Nat. Med. 4: 285-290; and Calissano and Macino, 1996, Fungal Genet. Newslett. 43: 15-16, Tian et al, 2004, Nature 432: 1050-1054; Reidhaar-Olson and Sauer, 1988, Science 241 : 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156; WO 95 / 17413; or WO 95 / 22625, Lowman et al., 1991, Biochemistry 30: 10832-10837; U.S. Patent No. 5,223,409; WO 92 / 06204, Derbyshire et al., 1986, Gene 46: 145; Ner et al., 1988, DNA 7: 127.Nucleic acid constructThe present invention also refers to a polynucleotide encoding the apolipoprotein of the present invention. Preferably, the polynucleotide is a codon-optimized polynucleotide for improving expression in a specific host cell, preferably a Bacillus cell, more preferably a B. licheniformis cell.The present invention thus also refers to a polynucleotide, preferably a purified, a synthetic, and / or a recombinant polynucleotide comprising:(a) a polynucleotide having with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, or SEQ ID NO: 21 , wherein the polynucleotide encodes an apolipoprotein;(b) a polynucleotide encoding an apolipoprotein having with increasing preference at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6;(c) a polynucleotide that hybridizes under high stringency conditions, preferably under very high stringency conditions, with the complement of(i) a coding sequence of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6; or(ii) a polynucleotide shown in SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 21 , SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, or SEQ ID NO: 20;(d) a fragment of (a), (b), or (c), wherein the fragment encodes an apolipoprotein; or(e) a polynucleotide sequence fully complementary to any of (a) to (d).(f) a polynucleotide that differs from any of the nucleic acid sequences described in (a) to (e) merely by the degeneracy of the genetic code.In a further embodiment, the invention also relates to apolipoproteins which are encoded by a polynucleotide described herein, preferably purified, synthetic, or recombinant apolipoproteins, which are encoded by a polynucleotide described herein. Preferably, the apolipoprotein is encoded by a polynucleotide having with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 21 , SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, or SEQ ID NO: 20, preferably SEQ ID NO: 15, SEQ ID NO: 16, or SEQ ID NO: 21 , preferably SEQ ID NO: 15 or SEQ ID NO: 16, preferably SEQ ID NO: 15.In another embodiment, the apolipoprotein is encoded by a polynucleotide that hybridizes under high stringency conditions, preferably under very high stringency conditions, with the full-length complement of a polynucleotide having with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%,at least 98%, at least 99%, or 100% identity to SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 21 , SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, or SEQ ID NO: 20, preferably SEQ ID NO: 15, SEQ ID NO: 16, or SEQ ID NO: 21 , preferably SEQ ID NO: 15 or SEQ ID NO: 16, preferably SEQ ID NO: 15.In another embodiment, the apolipoprotein is encoded by a polynucleotide having with increasing preference at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 28, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, or SEQ ID NO: 27, preferably SEQ ID NO: 22, preferably SEQ ID NO: 22, SEQ ID NO: 23, or SEQ ID NO: 28, preferably SEQ ID NO: 22 or SEQ ID NO: 23, preferably SEQ ID NO: 22.The present invention also refers to a nucleic acid construct, preferably an expression cassette, comprising the polynucleotide as described herein.Typically, the expression cassette comprises three elements: a promoter sequence, an open reading frame and a 3' untranslated region that, in eukaryotes, usually contains a polyadenylation site. Additional regulatory elements may include transcriptional as well as translational enhancers. An intron sequence may also be added to the 5' untranslated region (UTR) or in the coding sequence to increase the amount of the mature message that accumulates in the cytosol. The expression cassette may be part of a vector or may be integrated into the genome of a host cell and replicated together with the genome of its host cell. The expression cassette usually is capable of increasing or decreasing expression.The present invention also refers to an expression vector comprising the polynucleotide or the nucleic acid construct as described herein. The expression vector can be a low copy number vector or high copy number vector.A vector as used herein may provide segments for transcription and translation of a foreign polynucleotide upon transformation into a host cell or host cell organelles. Such additional segments may include regulatory nucleotide sequences, one or more origins of replication that is required for its maintenance and / or replication in a specific cell type, one or more selectable markers, a polyadenylation signal, a suitable site for the insertion of foreign coding sequences such as a multiple cloning site etc. One example is when a vector is required to be maintained in a bacterial cell as an episomal genetic element (e.g., plasmid or cosmid molecule). Non-limiting examples of suitable origins of replication include the f1-ori and colE1.A vector may replicate without integrating into the genome of a host cell, e.g., as a plasmid in a bacterial host cell, or it may integrate part or all of its DNA into the genome of the host cell and thus lead to replication and expression of its DNA.The polynucleotide encoding the apolipoprotein of the present invention may be introduced into a vector by means of standard recombinant DNA techniques. Once introduced into the vector, the polynucleotide comprising a coding sequence may be suitable to be introduced (transformed, transduced, transfected, etc.) into a host cell or host cell organelles. A cloning vector may be chosen suitable for expression of the polynucleotide sequence in the host cell or host cell organelles.Host cellThe present invention also refers to a host cell comprising the polynucleotide encoding the apolipoprotein of the present invention, the nucleic acid construct as described herein, or the expression vector as described herein. In one embodiment of the invention, a vector is used for transformation of a host cell. Preferably, the host cell is capable of expressing the polynucleotide encoding the apolipoprotein of the present invention.The polynucleotide encoding the apolipoprotein of the present invention herein may be transiently or stably introduced into a host cell. The polynucleotide may be maintained non-integrated, for example, as a plasmid. Usually, stable transformation is due to integration of nucleic acid comprising a foreign coding sequence into the host cell chromosomes or as an episome (separate piece of nuclear DNA). Usually, transient transformation is due to nucleic acid comprising a foreign nucleic acid sequence not being integrated into the host cell chromosomes or as an episome. Methods for introducing a nucleic acid into a host cell are well-known in the art.Various host cells can be used for expressing the nucleic acid construct described herein. Preferably, the host cell of the present invention does not naturally express the apolipoprotein of the present invention. Thus, the host cell is preferably a recombinant host cell; the nucleic acid construct described herein is preferably heterologous to the host cell.In one embodiment, the host cell is a prokaryote or a eukaryote. The host cell may be a bacterium, an archaeon, a fungal cell, a yeast cell or a eukaryotic cell. In another embodiment, the host cell is a non-human host cell.Preferably, the host cell is a bacterial cell. The bacterial host cell may be any gram-positive bacterium or a gramnegative bacterium. Gram-positive bacteria include, but are not limited to, Bacillus, Brevibacterium, Corynebacterium, Streptococcus, Streptomyces, Staphylococcus, Enterococcus, Lactobacillus, Lactococcus, Clostridium, Geobacillus, and Oceanobacillus. Gram-negative bacteria include, but are not limited to, Escherichia, Pseudomonas, Salmonella, Campylobacter, Helicobacter, Acetobacter, Flavobacterium, Fusobacterium, Gluconobacter. In a specific embodiment the host cell is of the genus Escherichia or Bacillus. In a specific embodiment, the bacterial host cell is an Echerichia coli cell.Most preferably, the bacterial host cell is a Bacillus cell. Bacillus cells useful in the practice of the present invention include, but are not limited to, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus firmus, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus stearothermophilus, Bacillus methylotrophicus, Bacillus cereus Bacillus paralicheniformis, Bacillus subtilis, and Bacillus thuringiensis cells. In one embodiment, the bacterial host cell is a Bacillus amyloliquefaciens, Bacillus pumilus, Bacillus lentus, Bacillus licheniformis, Bacillus stearothermophilus or Bacillus subtilis cell. In preferred embodiment, the bacterial host cell is a Bacillus licheniformis cell, a Bacillus pumilus, or a Bacillus subtilis cell. Preferably, the bacterial host cell is a Bacillus licheniformis cell.Methods of makingThe apolipoprotein described herein can be produced at an industrial scale and subsequently purified. Industrial production of proteins is usually done by cultivating a host cell, which expresses the protein (also called fermentation). Suitable host cells are described above. A nucleic acid sequence encoding the apolipoproteindescribed herein can be transformed into the host cell, which is subsequently cultivated under conditions suitable for the host cell to produce the apolipoprotein. In a preferred embodiment, the apolipoprotein is purified from the host cell.Hence, in yet another embodiment, the present invention is directed to a method of producing an apolipoprotein comprising the steps of(a) providing a host cell comprising a recombinant nucleic acid construct comprising a polynucleotide encoding the apolipoprotein described herein by introducing the nucleic acid construct comprising the polynucleotide encoding the apolipoprotein as described herein into the host cell;(b) cultivating the recombinant host cell of step (a) under conditions conductive for the expression of the polynucleotide; and(c) optionally, recovering the apolipoprotein encoded by the polynucleotide.Cultivation of the host cell normally takes place in a suitable nutrient medium allowing the recombinant cells to grow and express the desired protein. At the end of fermentation, the fermentation broth is collected and may be further processed, wherein the fermentation broth comprises a liquid fraction and a solid fraction. The apolipoprotein may be further purified from the fermentation broth.The apolipoprotein described herein may be secreted (into the liquid fraction of the fermentation broth) or may not be secreted from the microbial cells (and therefore is comprised in the cells of the fermentation broth). Depending on this, the apolipoprotein may be recovered from the liquid fraction of the fermentation broth or from cell lysates. Preferably, the apolipoprotein is secreted from the cell into the fermentation broth, preferably by means of a secretion signal peptide (also called signal peptide herein) added to a terminus, preferably the amino terminus, of the amino acid sequence of the apolipoprotein.Various signal peptides known to those skilled in the art can be used for expressing the apolipoprotein of the present invention. In one embodiment, the signal peptide is the native signal peptide of the apolipoprotein to be expressed. In another embodiment, the signal peptide and the apolipoprotein are recombinant to each other, meaning they are naturally not occurring in the specific combination with each other.In one embodiment, the signal peptide is selected from the group consisting of wapA, ydjM, and yvcE (preferably, amino acid sequence: SEQ ID NO: 29, SEQ ID NO: 30, and SEQ ID NO: 31, respectively; preferably nucleic acid sequence: SEQ ID NO: 32, SEQ ID NO: 33, and SEQ ID NO: 34, respectively).Thus, in a preferred embodiment, the signal peptide is selected from a group consisting of(a) a peptide having with increasing preference at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 29, SEQ ID NO: 30, or SEQ ID NO: 31, wherein the peptide has the function of a signal peptide; and(b) a peptide encoded by a polynucleotide having with increasing preference at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to SEQ ID NO: 32, SEQ ID NO: 33, or SEQ ID NO: 34, wherein the peptide has the function of a signal peptide.In a preferred embodiment, the signal peptide is wapA. Thus, in a preferred embodiment, the signal peptide is a peptide having with increasing preference at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 29, wherein the peptide has the function of a signal peptide.In another embodiment, in a preferred embodiment, the signal peptide is a peptide having with increasing preference at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 41 , SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, or SEQ ID NO: 40, wherein the peptide has the function of a signal peptide.Recovery of the apolipoprotein can be achieved by methods known to those skilled in the art. Suitable methods for recovery of proteins from fermentation broth include but are not limited to collection, centrifugation, filtration, extraction, and precipitation. In case the desired protein is comprised in the cells of the fermentation broth, release of the product of interest from the cells might be needed. Release from the cells can be achieved for instance, but not limited thereto, by cell lysis with techniques well known to the skilled person, e.g., lysozyme treatment, ultrasonic treatment, French press, or combinations thereof.The apolipoprotein may be purified from the fermentation broth by methods known in the art. For example, the apolipoprotein may be purified from the fermentation broth by conventional procedures including, but not limited to, centrifugation, filtration, extraction, spray-drying, evaporation, or precipitation. The isolated apolipoprotein may then be further purified by a variety of procedures known in the art including, but not limited to, chromatography (e.g., ion exchange, affinity, hydrophobic, chromatofocusing, and size exclusion), electrophoretic procedures (e.g., preparative isoelectric focusing (IEF)), differential solubility (e.g., ammonium sulfate precipitation), or extraction (see, e.g., Protein Purification, J.-C. Janson and Lars Ryden, editors, VCH Publishers, New York, 1989). The purified apolipoprotein may then be concentrated by procedures known in the art including, but not limited to, ultrafiltration and evaporation, in particular, thin film evaporation.Composition comprising apolipoproteinsThe purified solution of the apolipoprotein of the present invention may be further processed to form an apolipoprotein containing composition. Hence, also claimed herein is a composition comprising the apolipoprotein of the present invention and at least one additional component.Thus, the present invention therefore also refers to a method for making a composition comprising the steps of mixing i. an apolipoprotein as described herein; and ii. one or more components described herein.The composition can be a non-complex formulation, e.g., an apolipoprotein formulation, or a complex formulation, e.g., a cleaning composition, as described herein. The composition comprising the apolipoprotein can be an aqueous composition (with water being above 50% of all solvents), a low-water composition (with water being equal or below 50% of all solvents), or a non-aqueous composition (essentially free of water).The composition of the present invention can comprise more than one type of apolipoprotein.Apolipoprotein formulationIn one embodiment of the present invention, the apolipoprotein is formulated as an apolipoprotein formulation, preferably a concentrated apolipoprotein formulation. The apolipoprotein formulation can be either solid or liquid. Preferably the apolipoprotein formulation is liquid. Protein formulations can be obtained by using techniques known in the art. For instance, without being limited thereto, solid apolipoprotein formulations can be obtained by extrusion or granulation. Suitable extrusion and granulation techniques are known in the art and are described for instance in WO 94 / 19444 A1 and WO 97 / 43482 A1 .Apolipoprotein formulations, preferably liquid apolipoprotein formulations, may comprise amounts of apolipoprotein in the range of 1 % to 40%, 1 % to 30%, 1 % to 25%, 1 % to 12%, 1 % to 10%, 3% to 40%, 3% to 30%, 3% to 25%, 3% to 12%, or 3% to 10% by weight, all relative to the total weight of the apolipoprotein formulation.In one embodiment, the apolipoprotein formulation, in particular the liquid apolipoprotein formulation, comprises in addition one or more additional components selected from the group consisting of solvent, salt, pH regulator, preservative, stabilizer, and thickening agent. Preferably, the apolipoprotein formulation is essentially devoid of surfactants, i.e., the apolipoprotein formulation comprises less than 1 % surfactant, preferably less than 0.5% surfactant, more preferably 0% surfactant.The solvent may be water and / or an organic solvent. Aqueous apolipoprotein formulations of the invention may comprise water in amounts of more than about 30% by weight, more than about 40% by weight, more than about 50% by weight or more than about 60% by weight, all relative to the total weight of the apolipoprotein formulation. The apolipoprotein-containing formulations of the invention may comprise an organic solvent in amounts of more than 30%, more than 40%, more than about 50% by weight, more than about 60% by weight, more than about 70% by weight, or more than about 80% by weight, all relative to the total weight of the apolipoprotein formulation. The organic solvent may be a water-miscible solvent. The organic solvent may be one or more selected from the group consisting of glycerol, propanediol (in particular 1 ,2-propanediol (monopropylene glycol)), polypropylene glycol, or polyethylene glycol.In one embodiment, the apolipoprotein formulation comprises at least one preservative. Preferably, preservative means substances that are added to a liquid composition for the purpose of preservation, meaning more preferably that compounds known to have preserving features comprised in a liquid composition formed in the production process are excluded from the term preservatives. In one embodiment, the preservative is selected from the group consisting of 2-phenoxyethanol, glutaraldehyde, 2-bromo-2-nitropropane-1 ,3-diol, formic acid in acid form or as its salt, and 4,4'-dichloro 2-hydroxydiphenylether. Usually, the liquid compositions of the invention comprise at least one preservative in amounts below 10ppm, such as in amounts ranging from 2 ppm to 5% by weight relative to the total weight of the liquid composition. Preferably, the apolipoprotein formulation is free from preservatives, meaning that preservatives are comprised in amounts less than 1 ppm, preferably 0 ppm.Preferably, the apolipoprotein formulation comprises a stabilizing system. Preferably, the stabilizing system comprises at least one compound selected from the group consisting of polyols (preferably, 1 ,3-propanediol,ethylene glycol, glycerol, 1 ,2-propanediol, or sorbitol), inorganic salts (preferably, CaCh, MgCh, or NaCI), short chain (preferably, C1-C3) carboxylic acids or salts thereof (preferably, formic acid, formate (preferably, sodium formate), acetic acid, acetate, or lactate). In one embodiment, the stabilizing system comprises a combination of at least two of the compounds selected from the group consisting of salts, polyols, and short chain carboxylic acids or salts thereof. Preferably, the apolipoprotein formulation comprises a calcium salt, preferably calcium chloride.Preferably, the liquid apolipoprotein formulation comprises or consists of the apolipoprotein of the present invention, a solvent, a stabilizing system, and optionally a preservative and optionally an enzyme. Preferably, the formulation of the apolipoprotein of the present invention is essentially devoid of surfactants, i.e. the apolipoprotein formulation comprises less than 1 % surfactant, preferably less than 0.5% surfactant, most preferably 0% surfactant.The present invention therefore also relates to a method for making an apolipoprotein formulation, preferably a concentrated apolipoprotein formulation, comprising the steps of mixing a) an apolipoprotein of the present invention; and b) one or more components selected from the group consisting of solvent, stabilizing system, preservative, and optionally one or more enzymes.In one embodiment, the formulation is a formulation comprising a microorganism (alive, attenuated, or inactivated) containing the apolipoprotein of the present invention such as a probiotic or prebiotic formulation.EnzymesIn another embodiment, the composition comprising an apolipoprotein of the present invention further comprises one or more enzymes. Preferably, the enzyme is selected from the group consisting of proteases, amylases, lipases, cellulases, mannanases, hemicellulases, phospholipases, esterases, chitinases, lactases, peroxidases, xylanases, cutinases, keratinases, reductases, oxygenases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, beta-glucanases, arabinosidases, hyaluronidases, chondroitinases, laccases, nucleases, ribonucleases (RNAses), deoxyribonucleases (DNAses), phosphodiesterases, phytases, carbohydrases, galactanases, xanthanases, xyloglucanases, oxidoreductases, perhydrolases, aminopeptidases, asparaginases, carbohydrases, carboxypeptidases, catalases, chitinases, cyclodextrin glycosyltransferases, alpha-galactosidases, beta-galactosidases, glucoamylases, alpha-glucosidases, beta-glucosidases, invertases, transglutaminases and dispersins, and combinations of at least two of the foregoing types. More preferably, the enzyme is selected from the group consisting of proteases, amylases, lipases, cellulases, mannanases, esterases, xylanases, DNAses, dispersins, chitinases, oxidoreductases, and cutinases, and combinations of at least two of the foregoing types. Further preferred, the enzyme is selected from the group consisting of proteases, amylases, cellulases, mannanases, and combinations of at least two of the foregoing types. Most preferably, the enzyme is a protease.Cleaning compositionsIn one embodiment, the present invention is directed to the use of apolipoproteins in a cleaning composition. Thus, the present invention is also directed to a cleaning composition comprising the apolipoprotein of the present invention and one or more adjunct cleaning additive.The publication IPCCM000274907D published on www.IP.com is regarded as Reference RF1 , which is incorporated herein by reference in its entirety. The publication Prior Art Disclosure; Issue 684; paragraphs

[3000] to

[3061] ; ISSN: 2198-4786; published: February 12, 2024 is regarded as Reference RF2, which is incorporated herein by reference in its entirety.Preferably, the cleaning composition is for Fabric and Home Care. "Cleaning compositions” are defined in more detail in paragraphs

[0001] ,

[0002] ,

[0004] and

[0006] of Reference RF1."Compositions for Fabric and Home Care” include cleaning compositions and formulations including but not limited to laundry cleaning compositions and hard surface cleaning compositions, including dish washing compositions, more preferably liquid laundry formulations, solid laundry compositions, liquid manual dish wash formulations, automatic dish wash (ADW) gels and automatic dish wash (ADW) solid compositions. "Compositions for Fabric and Home Care” are defined in more detail in paragraph

[0003] of Reference RF1.The cleaning compositions of the invention including the apolipoprotein(s) may - and preferably do - contain adjunct cleaning additives (also abbreviated herein as "adjuncts”).Thus, in one embodiment, the additional component comprised in the composition comprising the apolipoprotein is an adjunct cleaning additive.Suitable adjunct cleaning additives include polymers, surfactants, builders, cobuilders, further enzymes, enzyme stabilizing systems, structurants or thickeners, clay soil removal / anti-redeposition agents, solubilizing agents, chelating agents, bleaching compounds, bleaching agents, bleach activators, bleach catalysts, brighteners, malodor control agents, pigments, dyes, opacifiers, hueing agents, dye transfer inhibiting agents, chelating agents, suds boosters, suds suppressors (antifoams), color speckles, silver care, anti-tarnish and / or anti-corrosion agents, alkalinity sources, pH adjusters, pH-buffer agents, hydrotropes, scrubbing particles, antibacterial agents, antioxidants, softeners, carriers, processing aids, pro-perfumes, dye fixation agent and perfumes.Thus, the present invention also relates to a method for making a cleaning composition comprising the steps of mixing a) an apolipoprotein of the present invention, preferably in the form of an apolipoprotein formulation, preferably liquid apolipoprotein formulation; and b) one or more adjunct cleaning additives described herein.Thus, the present invention also relates to a method for making a cleaning composition comprising the steps of mixing a) a liquid apolipoprotein formulation; and b) a cleaning composition.The addition of the liquid apolipoprotein formulation to a cleaning composition, preferably liquid cleaning composition, usually occurs in a weight ratio liquid apolipoprotein formulation:cleaning composition of about 1 : 1000,1 :500, 1 :100, 1 :50, 1 :30, 1 :25, 1 :20, or 1 :10. Preferably, the cleaning compositions comprise amounts of apolipoprotein in the range of 0.01 % to 0.80%, 0.01 % to 0.60%, 0.01% to 0.40%, 0.01% to 0.30%, 0.01% to 0.25%, 0.01 % to 0.12%, 0.01 % to 0.10%, 0.03% to 0.40%, 0.03% to 0.30%, 0.03% to 0.25%, 0.03% to 0.12%, or 0.03% to 0.10% by weight, all relative to the total weight of the cleaning composition.In one embodiment, the cleaning compositions comprise the apolipoprotein(s) and at least one polymer, preferably cleaning polymers and / or soil release polymers. "Cleaning polymers and soil release polymers” are defined in more detail in paragraphs

[0032] to

[0034] of Reference RF1. These polymers include polycarboxylates, alkoxylated polyalkylenamines, alkoxylated polyalkylenimines, polyether-based polymers, rheology-modifying polymers, dye inhibition polymers and soil release polymers as defined in more detail in paragraphs

[3035] to

[3044] of Reference RF2.Polymers may include, without limitation, "multifunctional alkoxylated polyethylene imines”, "multifunctional alkoxylated diamines” and also terephthalic acid-based polyesters like Clariant's TexCare®, such as TexCare® SRN 170, TexCare® SRN 172, TexCare® SRN 260, TexCare® SRN 260 SG Terra and TexCare® SRA 300 as well as distinct combinations of all of the before mentioned polymers. Also included are graft polymers comprising a polyalkylene oxide-based backbone with grafted side chains of vinyl ester monomer and optionally N- vinylpyrrolidone monomers.In an alternative embodiment, the cleaning composition does not comprise a polymer.In preferred embodiments, the cleaning compositions comprise the apolipoprotein(s) and at least one surfactant. "Surfactants” are anionic, non-ionic, cationic, amphoteric and zwitter-ionic surfactants defined in more detail in paragraphs

[3008] to

[3034] of Reference RF2. In addition, these surfactants are also described in more detail in paragraphs

[0007] to

[0013] of Reference RF1.Anionic surfactants for inventive cleaning compositions include linear alkylbenzenesulfonates (LAS), alkyl sulfates (AS), alkyl alkoxy sulfates (AES), alkyl alkoxy carboxylates, modified alkylbenzene sulfonate (MLAS), methyl ester sulfonate (MES), alkyl sulfosuccinates, alpha-olefin sulfonate (AOS), alkyl polyglycosides (APG) and biosurfactants, such as rhamnolipids and sophorolipids. Non-ionic surfactants for inventive cleaning compositions include alkoxylates, alkoxylated alcohols, alkoxylated fatty acids and alkoxylated (poly-)saccharides. Cationic surfactants for inventive cleaning compositions include surfactants comprising a quaternary ammonium. Amphoteric surfactants for inventive cleaning compositions include amine oxides. Zwitter-ionic surfactants for inventive cleaning compositions include betaines.In preferred embodiments, the cleaning compositions comprise the apolipoprotein(s) and at least one builder. "Builders” are defined in more detail in paragraphs

[0014] to

[0018] of Reference RF1. These builders include non- phosphate-based builders (NPB) and phosphonates (CoP) described in more detail in paragraphs

[3001] to

[3005] of Reference RF2.Builders may include, without limitation, methylglycinediaceticacid (MGDA), ethylenediaminedisuccinic acid (EDDS), glutamic acid diacetate (GLDA), citric acid and salts thereof.In preferred embodiments, the cleaning compositions comprise the apolipoprotein(s) and at least one enzyme. "Enzymes” are defined in more detail in paragraphs

[0020] to

[0027] of Reference RF1.These enzymes may include hydrolases, such as proteases, amylases, lipases, DNases, cellulases, hemicellulases, phospholipases, esterases, mannanases, xylanases, disperses, oxidoreductases, cutinases, chitinases, lactases, and peroxidases. In more preferred embodiments, the cleaning composition comprises, in addition to the apolipoprotein(s), an enzyme and an enzyme stabilizing system as described herein or in the chapter "Enzyme stabilizing system” of Reference RF1.In preferred embodiments, the cleaning compositions comprise the apolipoprotein(s) and at least one biocide. "Biocides” are defined in more detail in paragraphs

[0035] and

[0036] of Reference RF1. These biocides also include compounds as defined in more detail in paragraphs

[3006] and

[3007] of Reference RF2.Biocides may include, without limitation, 2-phenoxyethanol and 4,4'-dichoro 2-hydroxydiphenylether.Further adjunct cleaning additives are included and described in more detail in paragraphs

[0005] ,

[0019] ,

[0028] to

[0031] and

[0037] to

[0039] of Reference RF1.Liquid laundry formulations, solid laundry compositions, liquid manual dish wash formulations, automatic dish wash (ADW) gels and automatic dish wash (ADW) solid compositions comprising apolipoprotein(s) are defined in more detail in paragraph

[0044] of Reference RF1.Method of useThe apolipoprotein of the present invention or a composition comprising said apolipoprotein can be used in various applications such as in cleaning, as preservative, as antimicrobial, as insecticide, food processing, in the beverage industry, for juice extraction or juice processing, in the brewing industry, in animal feed, for pulp and paper processing, for baking, mining and oil extraction, in textile or leather processing, in water treatment, in ethanol production, for circular economy, in waste treatment, or recycling.The apolipoprotein of the present invention is preferably used in a cleaning composition.The apolipoprotein of the present invention is thus preferably used in any cleaning process such as laundry or hard surface cleaning, preferably for home care cleaning, l&l cleaning, floor cleaning, medical device cleaning, drain cleaning, membrane cleaning, biofilm removal, or automotive cleaning.The apolipoprotein of the present invention is preferably used in any cleaning process such as laundry or hard surface cleaning, preferably for home care or l&l cleaning.Thus, the present invention refers to a method for cleaning a textile or a hard surface comprising the steps of: a. exposing a textile or a hard surface to a cleaning composition comprising an apolipoprotein as described herein; b. completing at least one wash cycle; and c. optionally rinsing the textile or the hard surface.Thus, the present invention also refers to the use of an apolipoprotein as described herein for providing a cleaning composition with improved wash performance, preferably on apolipoprotein sensitive stains, preferably complex stains and / or stains comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains selected from sebum, lanoline,mayonnaise, fluid makeup, beef fat, vegetable fat, and lipstick stains, and / or bleachable stains, preferably, stains selected from fruit, vegetable, coffee, and ink stains.Thus, the present invention also refers to a method of using an apolipoprotein as described herein for brightening or for improving the whiteness of an object, preferably a textile or a hard surface.Thus, the present invention therefore also refers to a method for cleaning, preferably laundry or hard surface cleaning, comprising the step of contacting an object, preferably a textile or a hard surface, with a composition comprising an apolipoprotein of the present invention, preferably wherein the composition comprises at least one additional adjunct cleaning additive, preferably a surfactant and / or a builder. Preferably, the hard surfaces are selected from floors, furnishing, walls, sanitary ceramics, glass, metallic surfaces including medical devices, cutlery, and dishes. Preferably, the method for laundry cleaning, comprises the step of contacting a textile with a composition comprising an apolipoprotein as described herein, preferably wherein the composition comprises at least one adjunct cleaning additive, preferably a surfactant and / or a builder. Preferably, the method for hard surface cleaning, comprises the step of contacting a medical device, cutlery, or dish with a composition comprising an apolipoprotein as described herein, preferably wherein the composition comprises at least one adjunct cleaning additive, preferably a surfactant and / or a builder. A particular preferred form of hard surface cleaning is dishwashing, preferably manual dish washing (MDW) or automatic dishwashing (ADW), most preferably automatic dishwashing (ADW).The present invention also refers to the use of an apolipoprotein of the present invention for providing a cleaning composition with improved wash performance, preferably on apolipoprotein sensitive stains.In view of the cleaning performance of apolipoproteins, in particular on stains comprising one or more selected from fats, oils, and lipids, apolipoproteins as described herein can be used as substitutes for surfactants and / or polymers, in particular for polymers. Thus, the present invention also refers to the use of an apolipoprotein of the present invention for reducing the amounts of surfactants and / or polymers, preferably polymers, preferably non- biodegradable and / or non-biobased surfactants and / or non-biodegradable and / or non-biobased polymers, in a composition, preferably a detergent composition.Thus, the present invention also refers to the use of an apolipoprotein of the present invention for improving the biodegradability and / or the carbon-footprint of a composition, preferably a detergent composition.In view of apolipoproteins not having enzymatic activity and thus, do not cause malodorous catalytic reaction products, apolipoproteins, as described herein, can be used to reduce malodor formation in and / or after a cleaning step. Thus, the present invention also refers to the use of an apolipoprotein of the present invention for reducing malodor formation in and / or after a cleaning step, particularly in comparison with a cleaning step in which a detergent composition not comprising apolipoproteins, preferably comprising one or more lipase and / or one or more other lipolytic enzyme, is used.Thus, the present invention is also directed to a method of removing apolipoprotein sensitive stains, preferably complex stains and / or stains comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains selected from sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, and lipstick stains, and / or bleachable stains, preferably,selected from fruit, vegetable, coffee, and ink stains, comprising the step of contacting an object comprising a stain, preferably complex stains and / or stains comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains selected from sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, and lipstick stains, and / or bleachable stains, preferably, selected from fruit, vegetable, coffee, and ink stains, with a composition comprising an apolipoprotein comprising an amino acid sequence that is at least 60% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, as described herein.Thus, the present invention is also directed to a method of removing apolipoprotein sensitive stains, preferably stains comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains such as sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, or lipstick stains, comprising the step of contacting an object comprising a stain comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains such as sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, or lipstick stains, with a composition comprising an apolipoprotein comprising an amino acid sequence that is at least 60% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, as described herein.Thus, the present invention is also directed to a method of removing apolipoprotein sensitive stains, preferably stains comprising one or more chromophores, preferably complex stains comprising one or more chromophore, preferably bleachable stains, preferably, selected from fruits, vegetables, coffee, and ink stains, comprising the step of contacting an object comprising a stain comprising one or more chromophores, preferably complex stains comprising one or more chromophore, preferably bleachable stains, preferably, selected from fruits, vegetables, coffee, and ink stains, with a composition comprising an apolipoprotein comprising an amino acid sequence that is at least 60% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, as described herein.In one embodiment, the apolipoprotein of the present invention is used to improve the sustainability profile of a composition or a method and / or is used in circular economy. With respect to the use in circular economy, the apolipoprotein of the present invention can for instance be used in waste treatment or recycling.In one embodiment the present invention is directed to a process for waste treatment, preferably for solubilizing waste, comprising the step of contacting waste with an apolipoprotein of the present invention and preferably with one or more enzymes selected from the group consisting of protease, lipase, cellulase, glucanase, amylase, esterase and mannanase, under conditions supporting solubilizations of the waste. In one embodiment, the waste is municipal solid waste. In one embodiment, the liquified waste can be used as substrate for microbial fermentation.Preferred embodimentsWhile the invention has been illustrated and described in detail in the foregoing description, the description is to be considered illustrative or exemplary and not restrictive. The invention is not limited to the disclosedembodiments. Other variations to the disclosed embodiments can be understood and effected by those skilled in the art in practicing a claimed invention, from a study of the disclosure, and the dependent claims. The detailed description is merely exemplary in nature and is not intended to limit application and uses. The following examples further illustrate the present invention without, however, limiting the scope of the invention thereto. Various changes and modifications can be made by those skilled in the art on the basis of the description of the invention, and such changes and modifications are also included in the present invention.Preferred embodimentsSome preferred embodiments of the present invention include:1 . A composition comprising an apolipoprotein and at least one additional component, wherein the apolipoprotein preferably comprises an amino acid sequence that is at least 60% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1.2. The composition according to embodiment 1, wherein the apolipoprotein comprises an amino acid sequence that is with increasing preference at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1.3. The composition according to any of embodiment 1 or 2, wherein the apolipoprotein comprises an amino acid sequence that is at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 6.4. The composition according to any of embodiment 1 or 2, wherein the apolipoprotein comprises an amino acid sequence that is at least 98%, at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6.5. A composition according to any of embodiment 1 or 2, wherein the apolipoprotein comprises or consists of an amino acid sequence that is 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1.6. A composition according to any of embodiment 1 or 2, wherein the apolipoprotein comprises or consists of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6 or wherein the amino acid sequence of the apolipoprotein comprises or consists of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6 with 1-20 amino acid substitutions, preferably with 1-10 amino acid substitutions, or more preferably with 1-5 amino acid substitutions, preferably wherein the amino acid substitutions are conservative amino acid substitutions.The composition according to any of the previous embodiments, wherein the composition is a non-complex apolipoprotein formulation, preferably a liquid non-complex apolipoprotein formulation, wherein the additional component is preferably selected from the group consisting of solvent, salt, pH regulator, preservative, stabilizing system, and thickening agent. The composition according to embodiment 7, wherein the composition comprises a stabilizing system, wherein the stabilizing system preferably comprises at least one compound selected from the group consisting of polyols, preferably 1 ,3-propanediol, ethylene glycol, glycerol, 1,2-propanediol, or sorbitol, inorganic salts, preferably, CaCI2, MgCI2, or NaCI, and short chain carboxylic acids or salts thereof, preferably, formic acid, formate, preferably sodium formate, acetic acid, acetate, or lactate. The composition according to any of embodiments 7 or 8, wherein the composition comprises the apolipoprotein in an amount in the range of 1% to 40%, 1% to 30%, 1% to 25%, 1% to 12%, or 1% to 10% all relative to the total weight of the apolipoprotein formulation and wherein the composition is preferably liquid. The composition according to any of embodiments 1 to 6, wherein the composition is a complex composition, preferably a cleaning composition, preferably a laundry cleaning composition or a dish washing composition, more preferably a laundry cleaning composition. The composition according to embodiment 10, wherein the composition comprises the apolipoprotein in an amount in the range of 0.01% to 0.80%, 0.01% to 0.60%, 0.01% to 0.40%, 0.01% to 0.30%, 0.01% to 0.25%, 0.01% to 0.12%, 0.01% to 0.10% by weight, all relative to the total weight of the cleaning composition. The composition according to any of embodiment 10 or 11, wherein the at least one additional component is an adjunct cleaning additive, preferably selected from the group consisting of surfactants, builders, polymers, bleaching systems, fluorescent whitening agents, suds suppressors, enzymes, stabilizers, hydrotropes, rheology modifiers, preservatives, fragrances, and corrosion inhibitors, preferably selected from the group selected from surfactants and builders. The composition according to any of embodiments 10 to 12, wherein the composition comprises a surfactant and a builder. The composition of any of embodiments 1 to 13, further wherein the composition comprises at least one enzyme selected from the group consisting of protease, oxidoreductase, transferase, hydrolase, lyase, isomerase, ligase, aminopeptidase, amylase, asparaginase, carbohydrase, carboxypeptidase, catalase, cellulase, chitinase, cutinase, cyclodextrin glycosyltransferase, deoxyribonuclease, endo-beta 1,3 glucanase, endo-beta 1,4 glucanase, xanthan endoglucanase, esterase, alpha-galactosidase, betagalactosidase, glucoamylase, alpha-glucosidase, beta-glucosidase, glycosyl hydrolase, hyaluronic acid synthase, invertase, laccase, lipase, mannosidase, mutanase, oxygenase, peroxidase, phytase, polyphenoloxidase, pullulanase, ribonuclease, transglutaminase, dispersin, and xylanase, preferably, the at least one enzyme is selected from the group consisting of protease, amylase, cellulase, mannanase, lipase, dispersin, and DNase, more preferably, the at least one enzyme is selected from the group consisting of protease, amylase, cellulase, and mannanase, preferably a protease.A method of removing one or more stains, preferably apolipoprotein-sensitive stains, preferably complex stains and / or stains comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains selected from sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, and lipstick stains, and / or bleachable stains, preferably, selected from fruit, vegetable, coffee, and ink stains, comprising the step of contacting an object, preferably a textile or a hard surface, comprising one or more stains, preferably complex stains and / or stains comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains selected from sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, and lipstick stains, and / or bleachable stains, preferably, selected from fruit, vegetable, coffee, and ink stains, with a composition according to any of embodiments 1 to 14. Use of an apolipoprotein, preferably comprising an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1, for the removal of one or more stains, preferably Apolipoprotein sensitive stains, preferably complex stains and / or stains comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains selected from sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, and lipstick stains, and / or bleachable stains, preferably, selected from fruit, vegetable, coffee, and ink stains, from an object, preferably a textile or a hard surface, and / or for brightening and / or increasing whiteness of an object, preferably a textile or a hard surface. Use of an apolipoprotein, preferably comprising an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1, for reducing the amount of surfactants and / or polymers, preferably non- biodegradable and / or non-biobased surfactants and / or non-biodegradable and / or non-biobased polymers, in a composition, preferably a composition according to any of embodiments 1 to 14. Use of an apolipoprotein, preferably comprising an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1, for improving the biodegradability and / or the carbon-footprint of a composition, preferably a composition according to any of embodiments 1 to 14.Use of an apolipoprotein, preferably comprising an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1 , SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1 , for reducing malodor formation in and / or after a cleaning step, particularly in comparison with a cleaning step in which a detergent composition not comprising one or more apolipoproteins, preferably comprising one or more lipase and / or one or more other lipolytic enzyme, is used. A purified, synthetic, and / or recombinant apolipoprotein comprising an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 78%, at least 80%, at least 82%, at least 85%, at least 87%, at least 90%, at least 92%, at least 95%, at least 96%, at least 97%, at least 98% at least 99%, or 100% identical to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO:5, or SEQ ID NO: 6, preferably SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1 , SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1. An apolipoprotein according to embodiment 20, wherein the apolipoprotein comprises or consists of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1 , SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1 , or wherein the amino acid sequence of the apolipoprotein comprises or consists of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO:6, preferably SEQ ID NO: 1 , SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, preferably SEQ ID NO: 1 , with 1-20 amino acid substitutions, preferably with 1-10 amino acid substitutions, or more preferably with 1-5 amino acid substitutions, preferably wherein the amino acid substitutions are conservative amino acid substitutions. A purified, synthetic, and / or recombinant polynucleotide encoding the apolipoprotein according to any of embodiment 20 or 21 , preferably wherein the purified, synthetic, and / or recombinant polynucleotide preferably has at least 60% sequence identity to SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 21 , SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, or SEQ ID NO: 20, preferably SEQ ID NO: 15, SEQ ID NO: 16, or SEQ ID NO: 21 , preferably SEQ ID NO: 15 or SEQ ID NO: 16, preferably SEQ ID NO: 15. The polynucleotide according to embodiment 22, having with increasing preference at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 21, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, or, preferably SEQ ID NO: 15, SEQ ID NO: 16, or SEQ ID NO: 21 „ preferably SEQ ID NO: 15 or SEQ ID NO: 16, preferably SEQ ID NO: 15. A nucleic acid construct comprising the polynucleotide according to any of embodiments 22 or 23.25. An expression vector comprising the polynucleotide according to any of embodiments 22 or 23, or the nucleic acid construct according to embodiment 24.26. A host cell comprising the polynucleotide according to any of embodiments 22 or 23, the nucleic acid construct according to embodiment 24, or the expression vector according to embodiment 25.27. The host cell according to embodiment 26, wherein the host cell is a Bacillus cell, preferably a B. licheniformis cell.28. A method of making the apolipoprotein according to any of embodiments 20 or 21, comprising the steps of providing a polynucleotide encoding the apolipoprotein, transforming the polynucleotide into a host cell, cultivating the host cell, preferably a host cell according to any of the embodiments 26 or 27, to produce the apolipoprotein and optionally purifying the apolipoprotein.29. A method according to embodiment 28, wherein the apolipoprotein is secreted from the cell into the fermentation broth.30. A method according to embodiment 29, wherein the apolipoprotein is secreted by means of a signal peptide added to a terminus, preferably the amino terminus, of the amino acid sequence of the apolipoprotein.31. A method according to embodiment 30, wherein the apolipoprotein and the signal peptide are recombinant to each other.32. A method according to embodiment 31, wherein the signal peptide is selected from the group consisting of wapA, ydj M, and yvcE, preferably wapA.ExamplesExample 1 : Strain growth on agar plates with chicken feather media or sebum mediaBacterial strains from various sources were selected based on their habitats, with particular emphasis on Grampositive isolates from soil or human skin. All strains were first grown in commercially available tryptic soy broth, which was used to determine the viability of each strain and to seed the sebum and chicken feather agar assay plates (recipes below). For 100mm agar plates, a sterile loop was dipped into the seed culture and streaked out on the plate. When using 96-well agar plates, 10piL of seed culture was pipetted onto a single well of agar. All plates were incubated at 37°C for 48hr (Staphylococcus epidermidis ATCC 12228, Cutibacterium avidum ATCC 49768) or 28°C for up to 5 days (Brevibacillus sp. ATCC 29050, Streptomyces venezuelae ATCC 10712, and Streptomyces aureofaciens ATCC 10762).Samples were considered to pass the sebum agar assay if the area of the plate surrounding the bacterial colonies turned from pink to dark purple. Samples were considered to pass the chicken feather agar assay if colony growth was seen on the plate after 5 days incubation.Sebum agar assay plates were prepared using the following recipe:To 1L of Milli-Q water, 0.5g L-asparagine, 0.5g dibasic potassium phosphate, 10mg Iron(ll) sulfate heptahydrate, and 0.2g of magnesium sulfate heptahydrate was added. The solution was stirred until fully dissolved andautoclaved for 15 minutes at 121 °C. 10g of SASO Sebum (CFT Netherlands) and 4mL of Nile Red (resuspended at 2mg / mL in 100% ethanol) was added in a sterile fume hood and emulsified for 2-3 minutes. The solution was poured into sterile petri dishes, allowed to dry completely, and stored in the dark at 4°C until ready for use.Chicken feather assay plates were prepared using the following recipe:To 1L of Milli-Q water, 1.5g dibasic potassium phosphate, 25mg magnesium sulfate heptahydrate, 25mg calcium chloride, and 15mg Iron sulfate heptahydrate was added. The solution was stirred until fully dissolved, adjusted to pH 7.5 with hydrochloric acid and autoclave for 15 minutes at 121 °C. While still hot, 10g of chicken feather meal was added in a sterile fume hood and emulsified for 2-3 minutes. The solution was poured into sterile petri dishes, allowed to dry completely, and stored at 4°C until ready for use.The following strains were found to pass the sebum agar assay: Staphylococcus epidermidis ATCC 12228, Cutibacterium avidum ATCC 49768.The following strains were found to pass the chicken feather agar assay: Brevibacill us sp. ATCC 29050, Streptomyces venezuelae ATCC 10712 (Caracas, Venezuela), Streptomyces aureofaciens ATCC 10762 (Missouri, USA).Example 2: Liquid cultureSMM+S (sebum media) and SMM+G (glucose media) were prepared using the following recipe:To 1L of Milli-Q water, 0.5g L-asparagine, 0.5g dibasic potassium phosphate, 10mg Iron(ll) sulfate heptahydrate, and 0.2g of magnesium sulfate heptahydrate was added. The solution was stirred until fully dissolved and filtered using a 0.22 pm filter. 10g of carbon source (either glucose or molten synthetic sebum (from Scientific Services S / D, Inc., Sparrow Bush, NY, USA) was added in a sterile fume hood immediately prior to use and stirred well to combine.The following strains were cultured in sebum medium: Staphylococcus epidermidis ATCC 12228 and Cutibacterium avidum ATCC 49768Chicken feather media was prepared using the following recipe:To 1L of Milli-Q water, 0.5g sodium chloride, 0.4g monobasic potassium phosphate, and 0.3g dibasic potassium phosphate was added. The solution was stirred until fully dissolved and filtered using a 0.22pm filter. 10g of chicken feather meal was added in a sterile fume hood immediately prior to use and stirred well to combine. The following strains were cultured in chicken feather medium: Brevibacillus sp. ATCC 29050, Streptomyces venezuelae ATCC 10712, and Streptomyces aureofaciens ATCC 10762Seed cultures were generated by inoculating a single colony of the strain of interest into 10mL of tryptic soy broth and growing at either 37°C overnight (Staphylococcus epidermidis ATCC 12228, Cutibacterium avidum ATCC49768) or 28°C for 48hr (Brevibacillus sp. ATCC 29050, Streptomyces venezuelae ATCC 10712, and Streptomyces aureofaciens ATCC 1076,). 10OpiL of seed culture was used to inoculate either sebum or chicken feather liquid medium (depending on which assay the strain had passed) and a base media with glucose (SMM + G) (the latter for the proteomics analysis as described below). Samples were incubated for 48hr at either 37°C (Staphylococcus epidermidis ATCC 12228, Cutibacterium avidum ATCC 49) or 28°C for 72hr (Brevibacillus sp. ATCC 29050, Streptomyces venezuelae ATCC 10712, and Streptomyces aureofaciens ATCC 1076). Samples were spun down at 4000xg for 10 minutes at 4°C. The supernatant was removed and filtered through a 0.22 pm Steriflip filter (EMD Millipore).Sterile filtered supernatants were used for testing initial wash performance as described in Example 3. Supernatant samples of strains which showed wash performance in Example 3 were used for proteomics analysis as described in Example 4.Example 3: Initial wash performance using strain supernatant in miniaturized wash assay (mini wash)Wash experiments, using the supernatants as harvested under Example 2, were conducted for 60 minutes at 22°C in 50mL conical tubes rotating using 4g / L of a detergent blend (50% ES1-C and 50% Tide Hygienic Clean) as described in Table 1.Table 1 : Washing conditions miniaturized wash assay (mini wash)1) Producer: Center for Testmaterials BV, NL-3130 AC VlaardingenAfter the mini wash, the swatches were rinsed three times and dried flat overnight. The images were scanned and the RGB values were processed digitally. Wash performance is conveyed as the ARGB between the detergent with supernatant and the detergent alone control swatches (Table 2).Table 2: Wash performance in miniaturized assay (ARGB values)Supernatants from all five strains (Brevibacillus sp. 29050, S. venezuelae 10712, S. epidermidis 12228, C. avidum 49768, S. aureofaciens 10762) displayed brightening of sebum-stained fabric (WFK20D) when tested in mini wash assays described in Table 1. Therefore, supernatant samples of these strains were further evaluated by proteomics analysis.Example 4: Genomics and differential proteomicsBacterial strains (Brevibacillus sp. 29050, S. venezuelae 10712, S. epidermidis 12228, C. avidum 49768, S. aureofaciens 10762) were grown in tryptic soy broth and centrifuged as described in Example 2. Cell pellets were lysed and genomic DNA isolation was conducted using the MagMAX Microbiome DNA Isolation Kit and the King Fisher Apex system. All genomic DNA samples were cleaned using a 0.5X AmpureXP (Beckman Coulter) bead clean-up and prepared for sequencing using the Oxford Nanopore Ligation Barcoding 24 kit and associated protocol. Sequencing was done on the Oxford Nanopore MinlON system and FAST5 data were collected.Basecalling was done using the Oxford Nanopore Guppy software v6.5.7 and genome assembly was done using the Flye software for draft assembly followed by polishing with software programs Medaka v1 .11 and Racon v1.5.0. Initial genome annotations were done with the Prokka software v1 .14.5. Genome sequences and annotations were used as references for proteomics data generation.For proteomics sample preparations, samples were reconstituted in 200pil of_6M Guanidine-HCl. The samples were then boiled for 10 minutes followed by 5 minutes cooling at room temperature. The boiling and cooling cycle was repeated a total of 3 cycles. The proteins were precipitated with addition of methanol to final volume of 90% followed by vortex and centrifugation at maximum speed on a benchtop microfuge (14000 rpm) for 10 minutes.The soluble fraction was removed by flipping the tube onto an absorbent surface and tapping to remove any liquid. The pellet was suspended in 200pil of 8 M Urea made in 100mM Tris pH 8.0. TCEP (tris (2- carboxyethyl)phosphine) was added to final concentration of 10 mM and chloro-acetamide solution was added to final concentration of 40 mM and vortex for 5 minutes. 3 volumes of 50mM Tris pH 8.0 were added to the sample to reduce the final urea concentration to 2 M. Trypsin was added in 1 :50 ratio and incubated at 37°C for 12 hours. The solution was then acidified using TFA (0.5% TFA final concentration) and mixed. The sample was desalted using C18-StageTips (Thermo Fischer Scientific) as described by the manufacturer protocol. The peptide concentration of sample was measured using BCA. 0.200 pig of each sample were used for DIA analysis.For mass spectrometric acquisition for the construction of Data Independent Acquisition (DIA) library, _0.2 mg of each sample was analyzed by ultra-high pressure liquid chromatography (UPLC) coupled with tandem mass spectroscopy (LC-MS / MS) using nano-spray ionization. The nano-spray ionization experiments were performed using a TimsTOF 2 pro hybrid mass spectrometer (Bruker) interfaced with nano-scale reversed-phase UPLC (EVOSEP ONE). Evosep method 30 samples per day was utilized using a 15 cm x 150 pm reverse-phase column packed with 1.5 pm C18-beads (PepSep, Bruker) at 58 °C. The analytical columns were connected with a fused silica ID emitter (10 pm ID; Bruker Daltonics) inside a nanoelectrospray ion source (Captive spray source; Bruker). The mobile phases comprised 0.1% FA as solution A and 0.1% FA / 99.9% AON as solution B. The mass spectrometry setting for the TimsTOF Pro 2 are as following: PASEF (Parallel Accumulation Serial Fragmentation) method for standard proteomics. The values for mobility-dependent collision energy ramping were set to 95 eV at an inversed reduced mobility (1 / ko) of 1 .6 V s / cm2and 23 eV at 0.73 V s / cm2. Collision energies were linearly interpolated between these two 1 / ko values and kept constant above or below. No merging of TIMS scans was performed. Target intensity per individual PASEF precursor was set to 20 000. The scan range was set between 0.6 and 1 .6 V s / cm2with a ramp time of 166 ms. 14 PASEF MS / MS scans were triggered per cycle (2.57 s) with a maximum of seven precursors per mobilogram. Precursor ions in an m / z range between 100 and 1700 with charge states >3+ and <8+ were selected for fragmentation. Active exclusion was enabled for 0.4 min (mass width 0.015 Th, 1 / ko width 0.015 V s / cm2).Peptide identification was carried out using Peaks Studio 11 (Bioinformatics solutions Inc.). Peptides with FDR cutoff of 1% were selected for the DIA library file and mapped to the genome sequence for the organism.Proteins that were significantly differentially detected between samples grown in sebum / chicken feather as compared to samples grown in glucose media were selected. Selection was based on the degree of differential expression compared to cells grown on glucose medium. Known chaperones and housekeeping proteins were removed from consideration.Based on this analysis apolipoproteins as shown in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7 were identified.Example 5: Generation of B. licheniformis cells expressing apolipoproteins and small-scale expression of apolipoproteinsPlasmid DNA harboring the gene of an apolipoprotein as identified in Example 4 (protein sequence of apolipoproteins given in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7, nucleotide sequences used given in SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, and SEQ ID NO: 21) fused to the wapA, ydjM, or yvcE signal peptide from Bacillus subtilis (amino acid sequence: SEQ ID NO: 29, SEQ ID NO: 30, and SEQ ID NO: 31, respectively; nucleic acid sequence: SEQ ID NO: 32, SEQ ID NO: 33, and SEQ ID NO: 34, respectively) was used to transform chemically competent Bacillus licheniformis by electroporation. The transformed cells were incubated for 2 h at 37°C with shaking and then plated on an appropriate selection medium. The plate was incubated for 3 days at 26°C. Colonies of Bacillus licheniformis harboring the gene of apolipoproteins were picked and used to inoculate 0.6 ml of growth medium in a 96 well plate. The samples were incubated 16 h at 30°C or 37°C with shaking. This mature seed culture was diluted into an appropriate number of 0.6 ml aliquots in a 96 well plate, and the samples were incubated 48 h at 30°C or 37°C with shaking. The samples were clarified by centrifugation and the supernatant was harvested, aliquoted, and stored at -20°C. Concentrations of the apolipoproteins in the supernatants were determined by LabChip (see Table 3).Table 3: Expression levels determined using LabChipAs shown in Table 3, the apolipoproteins all showed good expression levels leading to a protein concentration of 0.07 to 4.21 mg / mL in the harvested supernatant.Example 6: Wash performance in miniaturized assay (mini wash)Wash experiments, using the apolipoproteins expressed under Example 5, were conducted for 60 minutes at 22°C in 50mL conical tubes rotating using 4g / L Tide Hygienic Clean detergent as described in Table 4.As a positive control, wash experiments were conducted using a cutinase enzyme (SEQ ID NO: 42), which was expressed under the same conditions.Table 4: Washing conditions in miniaturized assay (mini wash)1)Producer: Center for Testmaterials BV, NL-3130 AC VlaardingenAfter the wash run, the swatches were rinsed three times and dried flat overnight. The images were scanned and the RGB values were processed digitally. Wash performance is conveyed as the ARGB between the detergent with apolipoprotein and the detergent alone control swatches (Table 5).Table 5: Wash performance in the miniaturized wash assay (ARGB values)The addition of apolipoproteins having the sequences shown in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7 resulted in an improved wash performance on sebum stains. As can be derived from the table above, the addition of apolipoproteins displayed a similar increase in wash performance as the addition of a cutinase enzyme.Example 7: Wash performance in launder-o-meter (LOM)Apolipoproteins having SEQ ID NO: 1 , SEQ ID NO: 2, or SEQ ID NO: 7 were further tested in a laundry cleaning composition (ES1-C). A LOM wash assay was conducted in 5 g / l ES1-C formulation as set out in Table 6.Table 6: Washing conditions LOM essayWash assays were conducted in the cleaning composition ES1-C with detergent alone as the negative control. Apolipoproteins having SEQ ID NO: 1 , SEQ ID NO: 2, or SEQ ID NO: 7 were tested for wash performance. After the LOM run, the swatches were rinsed three times and dried flat overnight. The images were scanned and the RGB were processed digitally. Wash performance is conveyed as the ARGB between the detergent with apolipoprotein having SEQ ID NO: 1 , SEQ ID NO: 2, or SEQ ID NO: 7 and the detergent control swatches (Table 7). A cutinase (SEQ ID NO: 42) expressed under the same conditions and a commercially purchased lipase (SEQ ID NO: 43) were tested as positive references.Table 7: Results LOM assay using 5 g / L ES1-C detergentThe addition of apolipoproteins having the sequences shown in SEQ ID NO: 1, SEQ ID NO: 2, and SEQ ID NO: 7 resulted in an improved wash performance on a variety of stains, including fatty stains and bleachable stains. As can be derived from the table above, the addition of apolipoproteins displayed a similar increase in wash performance as the enzymes cutinase and lipase.Example 8: Wash performance in launder-o-meter (LOM)Apolipoproteins having SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7 were further tested in a commercial laundry cleaning composition (Dirty Labs). A LOM wash assay was conducted in 5 g / l Dirty Labs laundry detergent as set out in Table 8.Table 8: Washing conditions LOM essay1) Producer: Center for Testmaterials BV, NL-3130 AC VlaardingenWash assays were conducted in the cleaning composition Dirty Labs with detergent alone as the negative control. Apolipoproteins having SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7 were tested for wash performance. After the LOM run, the swatches were rinsed three times and dried flat overnight. The images were scanned and processed digitally. Wash performance is conveyed as the AE between the detergent with apolipoprotein having SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7 and the detergent alone control swatches. A cutinase (SEQ ID NO: 42) expressed under the same conditions and a commercially purchased lipase (SEQ ID NO: 43) were tested as positive references. The results are shown in Table 9.Table 9: Results LOM assay using 5 g / L Dirty Labs detergentAs can be derived from Table 9, the addition of apolipoproteins having the sequences shown in SEQ ID NO: 1 , SEQ ID NO: 2, and SEQ ID NO: 7 also resulted in an improved wash performance on a variety of stains even in a complex detergent formulation. As can be derived from the table above, the addition of apolipoproteins displayed a similar increase in wash performance as the enzymes cutinase and lipase.

Claims

CLAIMS1 . A cleaning composition comprising one or more apolipoproteins and at least one additional component.

2. The cleaning composition according to claim 1, wherein the cleaning composition is a laundry cleaning composition or a dish washing composition.

3. The cleaning composition according to any of claims 1 or 2, wherein the at least one additional component is selected from the group consisting of surfactants, builders, polymers, bleaching systems, fluorescent whitening agents, suds suppressors, enzymes, stabilizers, hydrotropes, rheology modifiers, preservatives, fragrances, and corrosion inhibitors.

4. The cleaning composition according to any of claims 1 to 3, wherein the composition comprises at least one enzyme selected from the group consisting of protease, oxidoreductase, transferase, hydrolase, lyase, isomerase, ligase, aminopeptidase, amylase, asparaginase, carbohydrase, carboxypeptidase, catalase, cellulase, chitinase, cutinase, cyclodextrin glycosyltransferase, deoxyribonuclease, endo-beta 1,3 glucanase, endo-beta 1,4 glucanase, xanthan endoglucanase, esterase, alpha-galactosidase, betagalactosidase, glucoamylase, alpha-glucosidase, beta-glucosidase, glycosyl hydrolase, hyaluronic acid synthase, invertase, laccase, lipase, mannosidase, mutanase, oxygenase, peroxidase, phytase, polyphenoloxidase, pullulanase, ribonuclease, transglutaminase, dispersin, and xylanase, preferably, the at least one enzyme is selected from the group consisting of protease, amylase, cellulase, mannanase, lipase, dispersin, and DNase, more preferably, the at least one enzyme is selected from the group consisting of protease, amylase, cellulase, and mannanase, preferably, a protease.

5. The cleaning composition according to any of claims 1 to 4, wherein the apolipoprotein comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, more preferably SEQ ID NO: 1.

6. A method for cleaning a textile or a hard surface comprising the steps of: a. exposing a textile or a hard surface to a cleaning composition according to any of claims 1 to 5; b. completing at least one wash cycle; and c. optionally rinsing the textile or the hard surface.

7. A method of removing one or more stains, preferably complex stains and / or stains comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains selected from sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, and lipstick stains, and / or bleachable stains, preferably, selected from fruit, vegetable, coffee, and ink stains, comprising the step of contacting an object comprising one or more stains, preferably complex stains and / or stains comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains selected from sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, and lipstick stains, and / or bleachable stains, preferably, selected from fruit, vegetable, coffee, and ink stains, with a cleaning composition according to any of claims 1 to 5.

8. Use of one or more apolipoproteins for the removal of one or more stains, preferably complex stains and / or stains comprising one or more selected from fats, oils, and lipids, preferably complex stains comprising one or more selected from fats, oils, and lipids, preferably stains selected from sebum, lanoline, mayonnaise, fluid makeup, beef fat, vegetable fat, and lipstick stains, and / or bleachable stains, preferably, selected from fruit, vegetable, coffee, and ink stains, from an object, preferably from a textile or a hard surface, and / or for brightening and / or increasing whiteness of an object, preferably a textile or a hard surface.

9. A purified, synthetic, and / or recombinant apolipoprotein comprising an amino acid sequence that is at least 60% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 6, preferably SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably SEQ ID NO: 1 or SEQ ID NO: 2, more preferably SEQ ID NO: 1.

10. The apolipoprotein according to claim 9, wherein the apolipoprotein comprises an amino acid sequence that is at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6, preferably at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7, preferably at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 1 or SEQ ID NO: 2, most preferably at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 1.

11. The apolipoprotein according to any of claim 9 or claim 10, wherein the amino acid sequence of the apolipoprotein comprises or consists of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6 or wherein the amino acid sequence of the apolipoprotein comprises or consists of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 7, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6 with 1-20 amino acid substitutions, preferably with 1-10 amino acid substitutions, or more preferably with 1-5 amino acid substitutions, preferably wherein the amino acid substitutions are conservative amino acid substitutions.

12. A formulation comprising the apolipoprotein according to any of claims 9 to 11 and at least one additional component, wherein preferably the at least one additional component is selected from the group consisting of solvent, salt, pH regulator, preservative, stabilizer, and thickening agent, preferably wherein the formulation is a liquid formulation.

13. A purified, synthetic, and / or recombinant polynucleotide encoding the apolipoprotein according to any of claims 9 to 11, wherein the purified, synthetic, and / or recombinant polynucleotide preferably has at least 60% sequence identity to SEQ ID NO:15, SEQ ID NO: 16, SEQ ID NO: 21, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, or SEQ ID NO: 20, preferably SEQ ID NO:15, SEQ ID NO: 16, or SEQ ID NO: 21, preferably SEQ ID NO:15 or SEQ ID NO: 16, preferably SEQ ID NO:15.

14. A host cell comprising the polynucleotide according to claim 13, wherein preferably the host cell is a Bacillus cell.

15. A method of making the apolipoprotein according to any of claims 9 to 11, comprising the steps of providing a polynucleotide encoding the apolipoprotein, transforming the polynucleotide into a host cell, cultivating the host cell to produce the apolipoprotein and optionally purifying the apolipoprotein.

Images