Means and methods for modifying trichothecene

Abstract

The present invention relates to a method for modifying a trichothecene, a composition comprising at least one polypeptide having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, and use of said polypeptide.

Description

MEANS AND METHODS FOR MODIFYING TRICHOTHECENE

[0001] The present invention relates to a method for modifying at least one trichothecene, a composition comprising at least one polypeptide, and use of said polypeptide.

[0002] Mycotoxins are secondary metabolites produced by various fungal species. Such fungi infest food as well as feed material, in particular all types of grains and feed crops, or other commodities such as cotton, coffee, peanuts, dates, spices etc. Upon fungal growth, mycotoxins such as aflatoxins, ochratoxin, ergot alkaloids, fumonisins, zearalenone and / or trichothecenes are produced, contaminating the infested material.

[0003] Among more than 17,000 samples, almost three quarters were found to contain at least one mycotoxin, and more than half of all samples contained one or more trichothecenes (Streit et al. 2013. J Sci Food Agric. 93(12): 2892-2899). Deoxynivalenol (DON; also referred to as vomitoxin; CAS-No. 51481-10-8) is one of the most prevalent trichothecenes. Feed contaminated with DON leads to feed refusal and reduced body weight gain and thus not only affects animal health and wellbeing but also causes considerable economic losses in animal farming.

[0004] To some extent, the degree of contamination can be reduced by maintaining "good agricultural practice", by avoiding moisture as much as possible to disfavor fungal growth, or by applying fungicides to the infested material. Additionally, contaminated material should be removed and discarded prior to processing. However, due to the high prevalence and to the low median toxic dose, further measures have to be considered.

[0005] Transformation of DON to its isomer, 3-epi-DON, has been described as an effective measure for DON detoxification (Bracarense et al. 2020. Food Chem Toxicol. 140: 111241). In the case of DON, the hydroxy group at carbon atom 3 is in R-configuration, whereas in the case of 3-epi-DON, the hydroxy group at carbon atom 3 is in S-configuration. The detoxification transformation from DON to 3-epi-DON has been described previously as a two-step-mechanism via the intermediate trichothecene 3-keto-DON (Carere et al. 2018. Microb Biotechnol. 11 (6): 1106-1111 ; Carere et al. 2018. Front Microbiol. 9:1573; He et al. 2020. Food Chem. 321 :126703). These described mechanisms rely on a pyrroloquinoline quinone (PQQ)-dependent dehydrogenase for DON oxidation to form 3-keto-DON with a carbonyl group on carbon 3, and one or more reductases to reduce 3-keto-DON to 3-epi-DON. Notably, some enzymes capable of using 3-keto-DON as a substrate catalyze a reduction reaction which at least partially leads back to DON rather than to the detoxified isomer 3-epi-DON. In addition, the oxidation reaction requires free PQQ, and the reduction reaction depends on the nicotine amide cofactor NADPH (reduced nicotinamide adenine dinucleotide phosphate). Even though these reactions can be quiteefficient, the dependence on two or even three enzymes and at least two further substrates, PQQ and NADPH, renders these mechanisms rather complex and therefore challenging to be applied e.g. as a detoxification additive for food or feed. Furthermore, NADPH is an acid-labile and relatively unstable molecule prone to rapid oxidation, and would have to be supplied in a constant, continuous matter, or regenerated by a cofactor regeneration system to ensure that the entire epimerization takes place in the intended field. Such a cofactor regeneration system could consist of at least one enzyme that uses the oxidized cofactor NADP+, to regenerate NADPH. Notably, in vivo application of such a system is challenging due to limited NADP(H) availability and stability. Thus, even though these published mechanisms ultimately produce 3-epi-DON, they are accompanied by several obstacles with regard to applicability. In particular, these published mechanisms are dependent on several cofactors and require a large number of enzymes.

[0006] In view of the prior art as outlined above, it is an objective of the present invention to provide means and methods for modifying trichothecenes such as DON or 3-keto-DON to form less toxic trichothecene derivatives.

[0007] This objective is achieved by providing a method for modifying (e.g. detoxifying) at least one trichothecene, comprising the step of forming a reaction mixture by contacting at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34, with a nutritional composition comprising the at least one trichothecene, and with NAD(H) and / or NADP(H), preferably with NAD(H). When performing such a method, detoxification of trichothecenes can be achieved. In particular, modification of DON to form the less toxic 3-keto- DON can be achieved, and / or modification of 3-keto-DON to the less toxic 3-epi-DON can be achieved.

[0008] A nutritional composition as referred to herein is a composition comprising one or more component(s) having nutritional value. Often such components provide energy to the consumer of the nutritional composition. A nutritional composition may be entirely or at least partly herbal or plant-based, such as commonly used animal feed compositions. In a preferred embodiment, the at least one polypeptide is comprised in the reaction mixture at a concentration of at least 0.1 mM. Most preferably, the at least one polypeptide is comprised in the reaction mixture at a concentration of at least 1 mM. In some embodiments, the at least one polypeptide is comprised in the reaction mixture at a concentration of 1.0, 1.1 , 1.2, 1.3, 1.4 or 1.5 mM.

[0009] The term "polypeptide" is to be construed as commonly used in the art and encompasses e.g. polypeptides, proteins, peptides, enzymes.

[0010] The term "sequence identity" is used to describe the degree of relatedness of two or more nucleic acid sequences (e.g. DNA or RNA polynucleotides) comprised in polynucleotides or of two or more amino acid sequences comprised in polypeptides. The sequence identity can be determined by common methods known to a skilled person. Herein, the preferred method for determination of sequence identity among two amino acid sequences comprised in two polypeptides is the use of the Clustal Omega alignment tool of EMBL-EBI (https: / / www.ebi.ac.uk / Tools / msa / clustalo / ; Sievers et al. 2011. Mol. Syst. Biol. 7: 539) with default settings. Alternatively, the Needleman-Wunsch algorithm for global sequence alignment may be used, e.g. as provided by the National Center for Biotechnology Information (“Needleman- Wunsch Global Align Protein Sequences”) using default settings (Gap Costs: Existence: 11 Extension 1). Polypeptides comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence of a target polypeptide may be polypeptides comprising an amino acid sequence having 70% or more % sequence identity, e.g. 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81 %, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 100% sequence identity to the amino acid sequence of the target polypeptide. For instance, a polypeptide comprising an amino acid sequence having 100% sequence identity to SEQ ID NO: 1 , is encompassed by the group of "polypeptides comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO: 1". It is common practice in the art to form fusion polypeptides linking one or more peptide tag(s) to the N- and / or C-terminus of a polypeptide, e.g. in order to facilitate easier purification or to increase solubility, without essentially altering the enzymatic properties of the tagged polypeptide. Typically, the term "fusion polypeptide" or "fusion protein" describes two or more polypeptide chains linked to one another, typically by peptide bonds. Examples for commonly used tags are poly(His)-tags (e.g. hexahistidine tag), maltose- binding-protein (MBP)-tag, Strep-tag, Strep ll-tag etc. Thus, enzymatically active fusion polypeptides comprising a polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34, are encompassed by the present invention. Such fusion polypeptides may e.g. comprise a hexahistidine tag fused to the N-terminus of a polypeptide comprising an amino acid sequence having 91 % sequence identity to the amino acid sequence of SEQ ID NO: 1 , or e.g. comprise a maltose-binding-protein tag fused to the C-terminus of a polypeptide comprising an amino acid sequence having 100% sequence identity to the amino acid sequence of SEQ ID NO: 34 via a linker peptide (e.g. GG; GPG; EAEA; GGSG; GGGGS; GSPAG; etc.). In other words, larger polypeptides comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34, as a part of said larger polypeptide are alsoencompassed by the present invention, as long as the enzymatic activity of said amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34, is not essentially obliterated. Merely for the sake of clarification, the enzymatically active polypeptide(s) according to the invention are capable of and thus suitable for modifying at least one trichothecene.

[0011] "NAD(H)" refers to the oxidized form, i.e. NAD+, and to the reduced form, i.e. NADH, of the cofactor nicotinamide adenine dinucleotide. "NADP(H)" refers to the oxidized form, i.e. NADP+, and to the reduced form, i.e. NADPH, of the cofactor nicotinamide adenine dinucleotide phosphate. In preferred embodiments of the method, the cofactor with which the at least one polypeptide and the nutritional composition are contacted is NAD+and / or NADH.

[0012] In some embodiments of the invention, the at least one trichothecene is deoxynivalenol and / or 3-keto-deoxynivalenol.

[0013] In some embodiments, the method according to the invention comprises the step of incubating the reaction mixture at a temperature between 5 °C and 40 °C, preferably at a temperature between 20 °C and 40 °C. In a preferred embodiment, the reaction mixture is incubated at body temperature, e.g. between 35 °C and 40 °C. Preferably said step of incubating the reaction mixture is performed for at least 5 minutes, preferably for at least 10 min (e.g. at least 15 min, 30 min, 60 min etc.). The longer the step of incubating the reaction mixture is performed, the more trichothecene will be modified. Notwithstanding, a skilled person is aware that an enzymatic type of reaction as described herein may also be effected outside said preferred conditions. Merely for the sake of clarity, incubation is considered to start immediately upon contact of a polypeptide according to the invention with a nutritional composition comprising the at least one trichothecene. A skilled person is well capable of choosing incubation conditions appropriate to modify a trichothecene concentration in a composition to a desired degree.

[0014] In some embodiments, the at least one trichothecene is deoxynivalenol, and the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1- 2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1. In particular, the at least one trichothecene is deoxynivalenol, and the at least one polypeptide has at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33, preferably to the amino acid sequence of SEQ ID NO: 1. Such polypeptides are particularly efficient in transforming DON to 3-keto-DON.

[0015] In some embodiments, the at least one trichothecene is 3-keto-deoxynivalenol, and the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34. In particular, the at least one trichothecene is 3-keto-deoxynivalenol, and the at least one polypeptide has at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54, preferably to the amino acid sequence of SEQ ID NO: 34. Such polypeptides are particularly efficient in transforming 3-keto-DON to 3-epi-DON.

[0016] In a preferred embodiment of the method according to the invention, a first trichothecene is deoxynivalenol, and a first reaction mixture is formed by contacting a nutritional composition comprising deoxynivalenol with at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1- 33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1- 13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1 ; and a second trichothecene is 3-keto-deoxynivalenol, and a second reaction mixture is formed by contacting a nutritional composition comprising 3-keto-deoxynivalenol with at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34. In a particular embodiment, a first trichothecene is deoxynivalenol, and a first reaction mixture is formed by contacting a nutritional composition comprising deoxynivalenol with at least one polypeptide having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1- 33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1- 13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1 ; and a second trichothecene is 3-keto-deoxynivalenol, and a second reaction mixture is formed by contacting a nutritional composition comprising 3-keto-deoxynivalenol with at least one polypeptide having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49,50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34.

[0017] In a particular embodiment, the method comprises a first step of contacting at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1- 2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1 , with a nutritional composition comprising deoxynivalenol and with NAD+, thus forming 3-keto-deoxynivalenol from the deoxynivalenol and forming NADH from the NAD+; and a second step of contacting the 3-keto-deoxynivalenol formed in the first step with at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34- 49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34, and contacting with NADH, preferably with the NADH formed in the first step; thus forming 3-epi-deoxynivalenol from the 3-keto-deoxynivalenol and forming NAD+from the NADH. In other words, in said particular embodiment, the invention relates to a method for modifying DON to form 3-epi-DON, comprising 1) forming 3-keto-DON and NADH by contacting at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1 , with a nutritional composition comprising deoxynivalenol and with NAD+; 2) forming 3-epi-DON and NAD+by contacting at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34- 44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34, with the 3-keto-DON formed in step 1) and with NADH, preferably with the NADH formed in step 1. Hereby, DON is first modified to 3-keto-DON while NAD+is reduced to NADH, and in a second step 3-keto-DON is reduced to form 3-epi-DON while NADH is recycled back to its oxidized form NAD+. Thus, the preferred cofactor NAD(H) canbe recycled and re-used in a further cycle of the method. Advantageously, such a method requires only at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1 , at least one further polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34- 41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34, and a NAD(H) cofactor, in order to repeatedly transform DON into 3-epi-DON.

[0018] In some embodiments, both, the at least one polypeptide consisting of or comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33, preferably to the amino acid sequence of SEQ ID NO: 1 , and the at least one polypeptide consisting of or comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54, preferably to the amino acid sequence of SEQ ID NO: 34, are each added to the nutritional composition to achieve a final concentration of at least 0.1 mM, preferably of at least 1 mM (e.g. of l .O, 1.1., 1.2, 1.3, 1.4 or 1.5 mM).

[0019] In another aspect, the invention relates to a composition (e.g. additive for food and / or feed; feed or food) for modifying (e.g. detoxifying) at least one trichothecene, comprising at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, and / or 54), preferably selected from SEQ ID NOs: 1 and 34. Such a composition is capable of detoxifying trichothecenes such as DON and / or 3-keto-DON.

[0020] In some embodiments of the invention, the composition is essentially devoid of cofactor(s) other than NAD(H) and / or NADP(H), preferably the composition is essentially devoid of cofactor(s) other than NAD(H). In a particular embodiment, the composition is devoid of pyrroloquinoline quinone (PQQ; CAS no. 72909-34-3).

[0021] A composition according to the invention can be e.g. food additive(s); foodstuff additive(s); fodder additive(s); feed additive(s); nutritional supplement(s); intermediate(s) thereof; and / or mixture(s) thereof. Such compositions may comprise further components, e.g. prebiotic(s); and / or probiotic(s). Merely for clarification, fodder or feed may e.g. comprise or consist of corn, hay, straw litter, soy, or products obtained therefrom. Also, fodder or feed may comprise or consist of extruded feed products, e.g. pellets. Additives for food, foodstuff, fodder or feed are often used to improve or add properties to the foodstuff, fodder or feed. For instance, such additives may be added to improve organoleptic properties, e.g. to improve taste, smell, appearance, color of the food, foodstuff, fodder or feed. Also, additives may be added to improve palatability, nutrient availability, or to add probiotic microorganisms to the food, foodstuff, fodder or feed, or to add or enhance prebiotic activity of the food, foodstuff, fodder or feed. Also, such additives may be added to counteract potentially undesirable effects of the food, foodstuff, fodder or feed, such as removal or reduction of one or more undesirable components comprised in the food, foodstuff, fodder or feed.

[0022] In some embodiments, the composition further comprises a cofactor selected from NAD(H) and NADP(H). Hereby, the composition is independent from varying concentrations of exogenous NAD(H) / NADP(H) cofactor.

[0023] In a preferred embodiment, the composition comprises at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 1-54, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, 1-33, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably selected from SEQ ID NOs: 1 and 34; and NAD(H). NAD(H) has the advantage of being less acid-labile than NADP(H), and of being a more stable molecule. In a particular embodiment, the composition comprises at least one polypeptide having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34; and NAD(H).

[0024] In some embodiments, the composition according to the invention comprises at least two polypeptides, wherein at least a first polypeptide comprises an amino acid sequence having at least 70% sequence identity to at least one amino acid sequence selected from SEQ ID NOs. 1- 33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1 ; and at least a second polypeptide comprises an amino acid sequence having at least 70% sequence identity to at least one amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34- 36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34. In a particular embodiment, the composition according to the invention comprises at least two polypeptides, wherein at least a first polypeptide has at least 70% sequence identity to at least one amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1- 20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1 ; and at least a second polypeptide has at least 70% sequence identity to at least one amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34- 48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34

[0025] In some embodiments, the composition of the invention further comprises at least one carrier. The carrier can be any suitable carrier. The composition may comprise one, two, three or even more carriers. The carrier may be dietary supplement(s), nutraceutical(s) and / or pharmaceutical(s), e.g. vitamin(s), mineral(s), amino acid(s), essential fatty acid(s), fiber(s), trace element(s), antioxidant(s), plant extract(s), herbal extract(s), and / or essential oil(s). The carrier can also be a carrier for enzyme(s). Carriers for enzymes can be both of inorganic and organic origin. Potential inorganic materials used for the immobilization of enzymes are silica (sol-gel silica, fumed silica, colloidal silica nanoparticles and silica gels) and oxides such as titanium oxide, aluminum oxide and zirconium oxide. Furthermore, clay materials such as bentonite, halloysite, kaolinite, montmorillonite, sepiolite and calcium apatite may be carriers. Additionally, carbonbased materials such as activated carbons and charcoal can be carriers. Organic enzyme carriers may be biopolymers (e.g. carbohydrates, proteins, maltodextrin, trehalose, inulin, collagen, cellulose, keratins, carrageenan, chitin, chitosan and alginate) or synthetic polymers (e.g. polyaniline, polyamides, polystyrene, polyurethane, polypropylene, polyvinyl alcohol and ion exchange resins). Liquid carriers could be e.g. buffer substances and / or polyalcohols such as polyalkylene oxides, polyvinyl alcohols, polyethylene-co-maleic acid anhydrides, polystyrene-co- malic acid anhydrides, dextrans, celluloses, hydrolyzates of chitosan, starches, glycogen, sorbitol,agarose and derivatives thereof, guar gum, pullulan, inulin, xanthan gum, carrageenan, pectin, alginic acid hydrolyzates, bio-polymers, sorbitol, glycerol, cellobiose, and mono propylene glycol. The carrier may additionally or alternatively be an eatable component, preferably a non-toxic component and / or a component providing for a texture. In a particular embodiment, the carrier is selected from bentonite, silica, and carbohydrates; preferably the carrier is bentonite.

[0026] In a further aspect, the invention relates to a use of at least one polypeptide in modifying a trichothecene, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

[0027] In some embodiments, the invention relates to a use of at least one polypeptide for modifying (in particular for detoxifying) a trichothecene, preferably deoxynivalenol, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1- 20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid of SEQ ID NO: 1.

[0028] In some embodiments, the invention relates to a use of at least one polypeptide for modifying (in particular for detoxifying) a trichothecene, preferably 3-keto-deoxynivalenol, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34- 51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid of SEQ ID NO: 34.

[0029] In some embodiments, the invention relates to a use of at least two polypeptides for modifying (in particular for detoxifying) a trichothecene, preferably deoxynivalenol and / or 3-keto- deoxynivalenol, wherein an at least first polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1- 14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid of SEQ ID NO: 1 ; and wherein an at least second polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid of SEQ ID NO: 34.

[0030] In a further aspect, the invention relates to a use of at least one polypeptide in manufacturing an additive for feed and / or food, a feed and / or food composition, or a pharmaceutical composition, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

[0031] In some embodiments, the invention relates to a use of at least one polypeptide in manufacturing an additive for feed and / or food, a feed and / or food composition, or a pharmaceutical composition, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1- 11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21, 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid of SEQ ID NO: 1.

[0032] In some embodiments, the invention relates to a use of at least one polypeptide in manufacturing an additive for feed and / or food, a feed and / or food composition, or a pharmaceutical composition, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41, 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid of SEQ ID NO: 34.

[0033] In some embodiments, the invention relates to a use of at least two polypeptides in manufacturing an additive for feed and / or food, a feed and / or food composition, or a pharmaceutical composition, wherein an at least first polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1- 11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21, 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31, 1-32, and / or 1-33), preferably to the amino acid of SEQ ID NO: 1; and wherein an at least second polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ IDNO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34- 36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid of SEQ ID NO: 34.

[0034] In another aspect, the invention relates to a use of at least one polypeptide in the manufacture of biogas; bioethanol, DDGS; sugar, preferably from sugar cane or sugar beets; corn oil, corn germs, corn germ meal, corn fibers, corn gluten, starch, in particular corn starch; and / or silage; wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

[0035] In some embodiments, the invention relates to a use of at least one polypeptide in the manufacture of biogas; bioethanol, DDGS; sugar, preferably from sugar cane or sugar beets; corn oil, corn germs, corn germ meal, corn fibers, corn gluten, starch, in particular corn starch; and / or silage; wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1- 32, and / or 1-33), preferably to the amino acid of SEQ ID NO: 1.

[0036] In some embodiments, the invention relates to a use of at least one polypeptide in the manufacture of biogas; bioethanol, DDGS; sugar, preferably from sugar cane or sugar beets; corn oil, corn germs, corn germ meal, corn fibers, corn gluten, starch, in particular corn starch; and / or silage; wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34- 49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid of SEQ ID NO: 34.

[0037] In some embodiments, the invention relates to a use of at least two polypeptides in the manufacture of biogas; bioethanol, DDGS; sugar, preferably from sugar cane or sugar beets; corn oil, corn germs, corn germ meal, corn fibers, corn gluten, starch, in particular corn starch; and / or silage; wherein an at least first polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid of SEQ ID NO: 1 ; and wherein an at least second polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34- 53, and / or 34-54), preferably to the amino acid of SEQ ID NO: 34.

[0038] In a further aspect, the invention relates to a host cell comprising at least one polypeptide and / or at least one polynucleotide encoding the at least one polypeptide, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 1-54, 1-2, 1-3, 1-4, 1- 5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, 1-33, 34-35, 34-36, 34-37, 34-38, 34- 39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably selected from SEQ ID NOs: 1 and 34. Such a host cell according to the invention allows production, in particular recombinant, heterologous production of the polypeptide(s) referred to herein.

[0039] In some embodiments, the invention relates to a host cell comprising at least two polypeptides, wherein an at least first polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1- 14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid of SEQ ID NO: 1 ; and wherein an at least second polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37,38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid of SEQ ID NO: 34.

[0040] The term "host cell" refers to any cell capable of recombinant protein production. In particular, "host cell" refers to prokaryotic and / or eukaryotic cells, preferably Pichia pastoris, Escherichia coli, Bacillus sp. such as e.g. Bacillus subtilis or Bacillus amyloliquefaciens, Streptomyces sp., Hansenula sp., Trichoderma sp., Lactobacillus sp., Aspergillus sp., plant cells and / or spores of Bacillus, Trichoderma or Aspergillus. Notably, strains commonly associated with"Pichia pastoris" are sometimes referred to as Komagataella pastoris, Komagataella phaffii or Komagataella pseudopastoris, depending on the respective taxonomic classification at the time of reference.

[0041] In another aspect, the invention relates to a polypeptide for modifying (e.g. detoxifying) at least one trichothecene comprising an amino acid sequence having at least 96.0% sequence identity to an amino acid sequence selected from SEQ ID NOs 1-22 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , and / or 1-22), preferably to SEQ ID NO: 1 ; or at least 91.0% sequence identity to an amino acid sequence selected from SEQ ID NOs 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34- 45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to SEQ ID NO: 34.

[0042] In some embodiments, the invention relates to a polypeptide for modifying (e.g. detoxifying) at least one trichothecene, in particular deoxynivalenol, comprising an amino acid sequence having at least 96.0% sequence identity to an amino acid sequence selected from SEQ ID NOs 1-22 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , and / or 1-22), preferably to SEQ ID NO: 1.

[0043] In some embodiments, the invention relates to a polypeptide for modifying (e.g. detoxifying) at least one trichothecene, in particular 3-keto-deoxynivalenol, comprising an amino acid sequence having at least 91 .0% sequence identity to an amino acid sequence selected from SEQ ID NOs 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34- 45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to SEQ ID NO: 34.

[0044] In a further aspect, the invention relates to at least one polypeptide for use in treatment, amelioration and / or prophylaxis of symptoms caused by mycotoxicosis, in particular by trichothecene mycotoxicosis, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

[0045] In some embodiments, the invention relates to at least one polypeptide for use in treatment, amelioration and / or prophylaxis of symptoms caused by mycotoxicosis, in particular by trichothecene mycotoxicosis (e.g. deoxynivalenol mycotoxicosis), wherein the at least onepolypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1- 2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid of SEQ ID NO: 1.

[0046] In some embodiments, the invention relates to at least one polypeptide for use in treatment, amelioration and / or prophylaxis of symptoms caused by mycotoxicosis, in particular by trichothecene mycotoxicosis (e.g. 3-keto-deoxynivalenol mycotoxicosis), wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34- 53, and / or 34-54), preferably to the amino acid of SEQ ID NO: 34.

[0047] In some embodiments, the invention relates to at least two polypeptides for use in treatment, amelioration and / or prophylaxis of symptoms caused by mycotoxicosis, in particular by trichothecene mycotoxicosis (e.g. deoxynivalenol and / or 3-keto-deoxynivalenol mycotoxicosis), wherein an at least first polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1- 14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid of SEQ ID NO: 1 ; and wherein an at least second polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37,38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid of SEQ ID NO: 34.

[0048] The invention is further characterized by the following items:

[0049] Item 1 : Method for modifying, e.g. detoxifying, at least one trichothecene, preferably deoxynivalenol (DON) and / or 3-keto-deoxynivalenol (3-keto-DON), comprising forming a reaction mixture by contacting at least one polypeptide comprising an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selectedfrom SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34, with a nutritional composition comprising the at least one trichothecene, and with NAD(H) and / or NADP(H), preferably with NAD(H).

[0050] Item 2. Method for modifying, e.g. detoxifying, at least one trichothecene, preferably deoxynivalenol (DON), comprising forming a reaction mixture by contacting at least one polypeptide comprising an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1- 32, and / or 1-33), preferably to the amino acid of SEQ ID NO: 1 , with a nutritional composition comprising the at least one trichothecene, and with NAD(H) and / or NADP(H), preferably with NAD(H).

[0051] Item 3. Method for modifying, e.g. detoxifying, at least one trichothecene, preferably 3- keto-deoxynivalenol (3-keto-DON), comprising forming a reaction mixture by contacting at least one polypeptide comprising an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34- 48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid of SEQ ID NO: 34, with a nutritional composition comprising the at least one trichothecene, and with NAD(H) and / or NADP(H), preferably with NAD(H).

[0052] Item 4. The method of any one of the preceding items, wherein the at least one polypeptide is capable of modifying a trichothecene, preferably at the C3 atom.

[0053] Item 5. The method of any one of the preceding items, wherein the at least one polypeptide is capable of modifying deoxynivalenol, preferably at the C3 atom.

[0054] Item 6. The method of any one of the preceding items, wherein the at least one polypeptide is capable of modifying 3-keto-deoxynivalenol, preferably at the C3 atom.

[0055] Item 7. The method of any one of the preceding items, wherein the method further comprises incubating the reaction mixture at a temperature of 5 - 40 °C, preferably at a temperature of 20 - 40 °C.

[0056] Item 8. The method of any one of the preceding items, wherein the step of incubating the reaction mixture is performed for at least 5 minutes, preferably for at least 10 minutes.

[0057] Item 9. The method of any one of items 1 , 2, 4, 5, 7, 8, wherein the at least one trichothecene is deoxynivalenol, and wherein the at least one polypeptide has at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1- 16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1.

[0058] Item 10. The method of any one of items 1 , 3, 4, 6-8, wherein the at least one trichothecene is 3-keto-deoxynivalenol, and wherein the at least one polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34- 52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34.

[0059] Item 11 . The method of any one of items 1 , 7, 8, wherein a first trichothecene is deoxynivalenol, and wherein a first reaction mixture is formed by contacting a nutritional composition comprising deoxynivalenol with at least a first polypeptide comprising an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1 ; wherein a second trichothecene is 3-keto-deoxynivalenol, and wherein a second reaction mixture is formed by contacting a nutritional composition comprising 3-keto-deoxynivalenol with at least a second polypeptide comprising an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34.

[0060] Item 12. The method of item 11 , wherein the at least first polypeptide is capable of modifying deoxynivalenol, preferably at the C3 atom, and wherein the at least second polypeptide is capable of modifying 3-keto-deoxynivalenol, preferably at the C3 atom.

[0061] Item 13. Method for modifying, e.g. detoxifying, at least one trichothecene, preferably deoxynivalenol (DON), comprising(i) forming 3-keto-deoxynivalenol (3-keto-DON) and NAD+, comprising contacting a nutritional composition comprising DON with at least a first polypeptide comprising an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33, preferably to the amino acid sequence of SEQ ID NO: 1 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1- 12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), with a nutritional composition comprising DON and with NAD+;(ii) forming 3-epi-deoxynivalenol (3-epi-DON) and NADH, comprising contacting 3-keto- DON, preferably the 3-keto-DON formed in (i), with at least a second polypeptide comprising an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34- 52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34, and with NADH, preferably with the NADH formed in (ii).

[0062] Item 14. The method of item 13, wherein the at least first polypeptide is capable of modifying deoxynivalenol, preferably at the C3 atom, and wherein the at least second polypeptide is capable of modifying 3-keto-deoxynivalenol, preferably at the C3 atom.

[0063] Item 15. The method of any one of items 11-14, wherein (i) and (ii) are performed at a temperature of 5 - 40 °C, preferably at a temperature of 20 - 40 °C.

[0064] Item 16. The method of any one of items 11-15, wherein (i) and (ii) each are performed for at least 5 minutes, preferably for at least 10 minutes.

[0065] Item 17. Composition, e.g. additive for food and / or feed; feed or food for modifying, e.g. detoxifying, at least one trichothecene, comprising at least one polypeptide comprising an aminoacid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 1-54, 1-2, 1-3, 1-4, 1- 5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, 1-33, 34-35, 34-36, 34-37, 34-38, 34- 39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably selected from SEQ ID NOs: 1 and 34.

[0066] Item 18. The composition of item 17, wherein the composition comprises a cofactor selected from NAD(H) and NADP(H), preferably NAD(H).

[0067] Item 19. The composition of item 17 or 18, wherein the composition comprises at least a first polypeptide comprising an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to at least one amino acid sequence selected from SEQ ID NOs. 1- 33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1- 13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NO: 1 ; and at least a second polypeptide comprising an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to at least one amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NO: 34.

[0068] Item 20. The composition of any one of items 17-19, wherein the composition comprises at least one carrier, preferably selected from bentonite, silica, and carbohydrates.

[0069] Item 21. The composition of any one of items 17-20, wherein the composition is a feed additive.

[0070] Item 22. Use of at least one polypeptide in modifying, in particular detoxifying, a trichothecene, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88,89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

[0071] Item 23. Use of at least one polypeptide in modifying, in particular detoxifying, a trichothecene, preferably DON, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NOs: 1.

[0072] Item 24. Use of at least one polypeptide in modifying, in particular detoxifying, a trichothecene, preferably 3-keto-DON, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82,83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34- 53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NOs: 34.

[0073] Item 24. Use of at least two polypeptides in modifying, in particular detoxifying, a trichothecene, preferably DON, wherein at least a first polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83,84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NOs: 1 ; and wherein at least a second polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34- 51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NOs: 34.

[0074] Item 25. The use of item 24, wherein the at least first polypeptide is capable of modifying, in particular detoxifying, DON, and wherein the at least second polypeptide is capable of modifying, in particular detoxifying, 3-keto-DON.

[0075] Item 26. Use of at least one polypeptide in manufacturing an additive for feed and / or food, a feed and / or food composition, or a pharmaceutical composition, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

[0076] Item 27. Use of at least one polypeptide in the manufacture of biogas; bioethanol, DDGS; sugar, preferably from sugar cane or sugar beets; corn oil, corn germs, corn germ meal, corn fibers, corn gluten, starch, in particular corn starch; and / or silage; wherein the at least one polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

[0077] Item 28. The use of any one of items 26-27, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1- 16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NOs: 1 .

[0078] Item 29. The use of any one of items 26-27, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34- 36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NOs: 34.

[0079] Item 30. The use of any one of items 26-27, wherein at least a first polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79,80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NOs: 1 ; and wherein at least a second polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34- 49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NOs: 34.

[0080] Item 31. Host cell comprising at least one polypeptide and / or at least one polynucleotide encoding the at least one polypeptide, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

[0081] Item 32. Polypeptide for modifying, e.g. detoxifying, at least one trichothecene, preferably DON and / or 3-keto-DON, comprising an amino acid sequence having at least 96.0% sequence identity to an amino acid sequence selected from SEQ ID NOs 1-22 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , and / or 1-22), preferably to SEQ ID NO: 1 ; or at least 91.0% sequence identity to an amino acid sequence selected from SEQ ID NOs 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34- 45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to SEQ ID NO: 34.

[0082] Item 33. Polypeptide for modifying, e.g. detoxifying, at least one trichothecene, preferably DON, comprising an amino acid sequence having at least 96.0% sequence identity to an amino acid sequence selected from SEQ ID NOs 1-22 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10,11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , and / or 1-22), preferably to SEQ ID NO: 1.

[0083] Item 34. Polypeptide for modifying, e.g. detoxifying, at least one trichothecene, preferably 3-keto-DON, comprising an amino acid sequence at least 91.0% sequence identity to an amino acid sequence selected from SEQ ID NOs 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to SEQ ID NO: 34.

[0084] Item 35. Composition comprising at least two polypeptides, wherein at least a first polypeptide comprises an amino acid sequence having at least 96.0% (e.g. at least 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs 1-22, preferably to SEQ ID NO: 1 ; and wherein at least a second polypeptide comprises an amino acid sequence having at least 91.0% (e.g. at least 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs 34-54, preferably to SEQ ID NO:34.

[0085] Item 36. Polypeptide for use in treatment, amelioration and / or prophylaxis or prevention of symptoms caused by mycotoxicosis, in particular by trichothecene mycotoxicosis, wherein the polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

[0086] Item 37. The polypeptide for use in treatment, amelioration and / or prophylaxis or prevention of symptoms caused by mycotoxicosis of item 36, wherein the polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NOs: 1 .

[0087] Item 37. The polypeptide for use in treatment, amelioration and / or prophylaxis or prevention of symptoms caused by mycotoxicosis of item 36, wherein the polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34,35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37,34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34-49, 34-50, 34- 51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NOs: 34.

[0088] Item 38. Polypeptide composition for use in treatment, amelioration and / or prophylaxis or prevention of symptoms caused by mycotoxicosis, wherein at least a first polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33 (e.g. SEQ ID NO(s): 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 1-2, 1-3, 1-4, 1-5, 1-6, 1-7, 1-8, 1-9, 1-10, 1-11 , 1-12, 1-13, 1-14, 1-15, 1-16, 1-17, 1-18, 1-19, 1-20, 1-21 , 1-22, 1-23, 1-24, 1-25, 1-26, 1-27, 1-28, 1-29, 1-30, 1-31 , 1-32, and / or 1-33), preferably to the amino acid sequence of SEQ ID NOs: 1 ; and wherein at least a second polypeptide comprises an amino acid sequence having at least 70% (e.g. at least 70, 71 , 72, 73, 74, 75, 76, 77, 78, 79, 80, 81 , 82, 83, 84, 85, 86, 87, 88, 89, 90, 91 , 92, 93, 94, 95, 96, 97, 98, 99, 100%) sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54 (e.g. SEQ ID NO(s): 34, 35, 36, 37, 38, 39, 40, 41 , 42, 43, 44, 45, 46, 47, 48, 49, 50, 51 , 52, 53, 54, 34-35, 34-36, 34-37, 34-38, 34-39, 34-40, 34-41 , 34-42, 34-43, 34-44, 34-45, 34-46, 34-47, 34-48, 34- 49, 34-50, 34-51 , 34-52, 34-53, and / or 34-54), preferably to the amino acid sequence of SEQ ID NOs: 34.Examples

[0089] In the following, the present invention is further described by non-limiting examples. The present invention as disclosed herein is not limited to specific embodiments, methodology, examples, protocols etc. described herein but solely defined by the claims.Example 1

[0090] For expression and protein purification of candidate genes, nucleotide sequences encoding polypeptides having any one of the amino acid sequences of SEQ ID NOs. 1-54 were cloned into plasmids for expression in a suitable host organism, in particular E. coli. The recombinant vectors were based on the E. coli expression vector pET28a with the nucleotide sequences containing the restriction site Ncol at the 5' end and the restriction site Xhol at the 3' end, as well as a 6xHis tag either on the C-terminal or the N-terminal end to facilitate affinity purification. Untagged enzymes were produced analogously and found to possess essentially identical enzymatic activities and protein characteristics.

[0091] E. coli BL21(DE3) was transformed with the recombinant pET28a-based expression vectors, and expression was induced with addition of IPTG. Cells were harvested by centrifugation and lysed by ultrasound or French Press treatment. Ultimately, any method known to a skilled person which is suitable to produce crude cell lysates from the employed host organism may be used. Alternative recombinant protein production hosts such as Bacillus-, Pseudomonas-, Pichia-, Yarrowia-, Streptomyces-, Hansenula-, Lactobacillus-, Saccharomyces- Aspergillus-, Trichoderma-based systems or others known in the art may be considered. The lysates were cleared by centrifugation and the supernatant comprising the soluble recombinant protein was assayed to determine the catalytic properties of the produced enzymes. Target protein concentration was determined via SDS-PAGE by comparison with Bovine Serum Albumin (BSA, Sigma #A4919) protein standards in concentrations from 100 pg / mL to 1500 pg / mL BSA.Example 2

[0092] To determine the suitability of the enzymes produced in Example 1 to modify a trichothecene substrate, the enzymes were tested in activity assays as described below.

[0093] The activity of DON oxidizing enzymes was tested in a standard DON degradation assay that is prepared as described in the following: 50 mM KPO4 buffer pH 5.4 - 8.0, 5 - 75 mg / L DON, 1.5 mM NAD(P)+, 2 mM MgCh, and 1 pM enzyme from cell lysate. Additionally, an NAD(P)H scavenger or an NAD(P)H-consuming enzyme may be added to accelerate the reaction. This NAD(P)H scavenger may be a quinone at a concentration of 1 mM, such as pyrroloquinoline quinone (PQQ), or small benzo- and naphtho-quinones like 1 ,4-benzoquinone, 2,6-dimethyl benzoquinone or 1 ,2-naphtoquinone. Alternatively, synthetic redox co-factors such as phenazine methosulfate (PMS), methylene blue, coenzymes Q10 and Q1 or potassium hexacyanoferrate (III) may be used as NAD(P)H scavenger. Instead or in addition, an enzyme which recycles NAD(P)+upon NAD(P)H consumption can be added to the reaction. Surprisingly and advantageously, enzymes having any one of the amino acid sequences of SEQ. ID NO. 34 - 54 were found capable of both, reducing NAD(P)H to form NAD(P)+as well as simultaneously oxidizing 3-keto-DON to form 3-epi DON, an even less toxic molecule than DON or than 3-keto- DON. In particular, enzymes having any one of the amino acid sequences of SEQ. ID NO. 34 - 54 were found capable of reducing NADH to form NAD+while oxidizing 3-keto-DON to form 3- epi-DON.

[0094] Practically, all components of the reaction except NAD(P)+ were mixed on ice and a 0 minutes sample was removed from the mixture. Immediately thereafter, reaction mixtures were transferred to the heating block and the reaction was started by adding the cofactor (i.e. the NAD+and / or NADP+) and allowed to react for 2-3 hours at 37 °C. Samples were removed in regular intervals in order to monitor the progression of the reaction and immediately mixed 1+1 (v / v) with 100% acetonitrile to stop the reaction. They were subsequently analyzed using the HPLC-MS / MS method described below.Example 3

[0095] Enzymes having any one of the amino acid sequences SEQ. ID NO. 1 -22 were tested for activity in an assay using expression culture lysate adjusted to OD 0.1 of cultures producing any one of the enzymes of SEQ ID NOs. 1-22. Comparability of expression levels was verified via SDS-PAGE analysis. To test for modification of DON to 3-keto-DON, these lysates were mixed with 37 mg / L DON, 1.5 mM NAD+, 2 mM MgCh, 0.1 mg / mL BSA. To test for further modification of 3-keto-DON to 3-epi-DON, these reaction mixtures were also mixed with expression culture lysate adjusted to OD 15 of a culture producing an enzyme having the amino acid sequence of SEQ. ID NO. 36 in 50 mM potassium phosphate buffer, pH 5.4. These final reaction mixtures were incubated at 37 °C and 100 rpm for 3 h, and the 3-epi-DON formation rate determined, see Table 1.Table 1 : Modification of DON to 3-keto-DON to 3-epi-DON.

[0096] To further study the ability of enzymes comprising an amino acid having at least 70% identity to the amino acid sequence of SEQ ID NO: 1 to modify DON as an exemplary trichothecene substrate, expression culture lysates of cultures producing any one of the enzymes of SEQ. IDs 23-33 as described in Example 1 were adjusted to OD 0.1 , and mixed with 25 mg / L DON, 1.5 mM NADP+, 1 mM of PQQ, in potassium phosphate buffer, pH 8. These reaction mixtures were incubated at 37 °C for 2 h, the formation of 3-keto-DON was followed, see Table 2.Table 2: Modification of DON to 3-keto-DON.

[0097] Notably, when comparing an enzyme for DON removal having an amino acid sequence of any one of SEQ ID NOs. 1-33, to the enzyme referred to as AKR18A1 by He et al. (2017. Sci Rep 7(1):9549), the latter was found to remove DON at least two times more slowly than any one of the former.

[0098] In addition, enzymes comprising an amino acid having at least 70% identity to the amino acid sequence of SEQ ID NO: 34 were tested for their ability to modify 3-keto-DON as a further exemplary trichothecene substrate. To this end, expression culture lysates of cultures producing any one of the enzymes of SEQ. IDs 34-54 as described in Example 1 , were adjusted to OD 1.5, and mixed with 37 mg / L DON, 1 .5 mM NAD+, 2 mM of MgCh, 0.1 mg / mL BSA in 50 mM potassium phosphate buffer, pH 6. Further addition of expression culture lysate adjusted to OD 15 of a culture producing the enzyme of SEQ ID NO: 1 in 50 mM potassium phosphate buffer, pH 6, allowed transformation of the available DON to form 3-keto-DON, thus initiating the reaction from 3-keto-DON to 3-epi-DON by any one of the enzymes of SEQ ID NOs. 34-54. These reactionmixtures were incubated at 37 °C at 100 rpm for 3 h, the formation of 3-epi-DON was followed, see Table 3.Table 3: Modification of 3-keto-DON to 3-epi-DON

[0099] Ultimately, all exemplarily tested enzymes were found capable of modifying at least one trichothecene mycotoxin. In detail, any one of the enzymes having any one of the amino acid sequences of SEQ ID NOs. 1-33 were found particularly well capable of modifying DON to form 3-keto-DON, while reducing NADP+. Most notably, the enzymes having any one of the amino acid sequences of SEQ ID NOs. 1-22 were found especially well capable of modifying DON to form 3- keto-DON, while reducing NAD+, thus allowing the use of the more stable cofactor NAD+rather than NADP+. Further, any one of the enzymes having any one of the amino acid sequences of SEQ ID NOs. 34-54 were found particularly well capable of modifying 3-keto-DON to form 3-epi- DON, while oxidizing NADH to form NAD+, thus facilitating recycling of the cofactor. Notably and in contrast to the enzymes having any one of the amino acid sequences of SEQ ID NOs. 34-54, enzymes previously described capable of reducing 3-keto-DON to form DON (e.g. in WO 2021 / 038026 A1) were not found suitable for recycling NADH to NAD+. Combinations of any one of the enzymes having any one of the amino acid sequences of SEQ ID NOs: 1-33, with any one of the enzymes having any one of the amino acid sequences of SEQ ID NOs: 34-54 allow formation of 3-epi-DON from DON via 3-keto-DON. A particularly efficient formation of 3-epi-DONfrom DON via 3-keto-DON was identified in combinations of any one of the enzymes having any one of the amino acid sequences of SEQ ID NOs: 1-22, with any one of the enzymes having any one of the amino acid sequences of SEQ ID NOs: 34-54 under recycling of NAD(H) as cofactor.Example 4

[0100] For HPLC analysis, samples were separated using a 150 mm x 4.6 mm Phenomenex Gemini-NX C18 column with a particle size of 5 pm. A mixture of acetonitrile and ultra-pure water was used a mobile phase and the UV-signal at 220 nm was recorded and evaluated in order to determine the concentrations of the trichothecene analytes, i.e. DON, 3-keto-DON and / or 3-epi- DON.

[0101] Alternatively or in addition, samples could be analyzed by LC-MS / MS. To this end, DON and its metabolites were separated on a 150 mm x 2.1 mm Phenomenex Kinetex Biphenyl column with a particle size of 2.6 pm. Prior to LC-MS / MS analysis all samples were diluted with 50% acetonitrile in water to a theoretical final concentration of 0.2 ppm DON in the sample. The mobile phase consisted of a mixture of methanol and ultrapure water with 0.1 % (v / v) acetic acid. Ions were generated using electro spray ionization (ESI) in negative ionization mode. The quantification is done using a QTrap and / or triple quadrupole mass detector. Samples need to be diluted to fall into the linear range of this method which ranges from analyte concentrations of 1 ppb to 500 ppb in the injected sample. The LOQ is the limit of reliable detection and concentrations below 1 ppb of compound detected in a sample are not considered as reliable and thus set to <LOQ.Example 6

[0102] To further compare exemplary enzymes according to the invention to one another, sequence alignments were performed. To this end, the Clustal Omega alignment tool of EMBL- EBI (https: / / www.ebi.ac.uk / Tools / msa / clustalo / ; Sievers et al. 2011. Mol. Syst. Biol. 7: 539) with default settings.

[0103] T able 5 below shows the identities of the amino acid sequences (T able 4) of 54 exemplary enzymes suitable for modifying trichothecenes.Table 4: Amino acid sequences.Table 5: Sequence identities of amino acid sequences of SEQ ID NOs: 1-54 to one another.

Claims

Claims1. Method for modifying, e.g. detoxifying, at least one trichothecene, comprising forming a reaction mixture by contacting at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1- 54, preferably selected from SEQ ID NOs: 1 and 34, with a nutritional composition comprising the at least one trichothecene, and with NAD(H) and / or NADP(H), preferably with NAD(H).

2. The method of claim 1 , wherein the method further comprises incubating the reaction mixture at a temperature of 5 - 40 °C, preferably at a temperature of 20 - 40 °C.

3. The method of any one of the preceding claims, wherein the step of incubating the reaction mixture is performed for at least 5 minutes, preferably for at least 10 minutes.

4. The method of any one of the preceding claims, wherein the at least one trichothecene is deoxynivalenol, and wherein the at least one polypeptide has at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33, preferably to the amino acid sequence of SEQ ID NO: 1.

5. The method of any one of claims 1-3, wherein the at least one trichothecene is 3-keto- deoxynivalenol, and wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54, preferably to the amino acid sequence of SEQ ID NO: 34.

6. The method of any one of claims 1-3, wherein a first trichothecene is deoxynivalenol, and wherein a first reaction mixture is formed by contacting a nutritional composition comprising deoxynivalenol with at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-33, preferably to the amino acid sequence of SEQ ID NO: 1 ; wherein a second trichothecene is 3-keto- deoxynivalenol, and wherein a second reaction mixture is formed by contacting a nutritional composition comprising 3-keto-deoxynivalenol with at least one polypeptide comprising an aminoacid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 34-54, preferably to the amino acid sequence of SEQ ID NO: 34.

7. Composition, e.g. additive for food and / or feed; feed or food, for modifying, e.g. detoxifying, at least one trichothecene, comprising at least one polypeptide comprising an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

8. The composition of claim 7, wherein the composition comprises a cofactor selected from NAD(H) and NADP(H), preferably NAD(H).

9. The composition of claim 7 or 8, wherein the composition comprises at least a first polypeptide comprising an amino acid sequence having at least 70% sequence identity to at least one amino acid sequence selected from SEQ ID NOs. 1-33, preferably to the amino acid sequence of SEQ ID NO: 1 ; and at least a second polypeptide comprising an amino acid sequence having at least 70% sequence identity to at least one amino acid sequence selected from SEQ ID NOs. 34-54, preferably to the amino acid sequence of SEQ ID NO: 34.

10. The composition of any one of claims 7-9, wherein the composition comprises at least one carrier, preferably selected from bentonite, silica, and carbohydrates.

11. Use of at least one polypeptide in modifying a trichothecene, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

12. Use of at least one polypeptide in manufacturing an additive for feed and / or food, a feed and / or food composition, or a pharmaceutical composition, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

13. Use of at least one polypeptide in the manufacture of biogas; bioethanol, DDGS; sugar, preferably from sugar cane or sugar beets; corn oil, corn germs, corn germ meal, corn fibers, corn gluten, starch, in particular corn starch; and / or silage; wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.

14. Host cell comprising at least one polypeptide and / or at least one polynucleotide encoding the at least one polypeptide, wherein the at least one polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1- 54, preferably selected from SEQ ID NOs: 1 and 34.

15. Polypeptide for modifying, e.g. detoxifying, at least one trichothecene comprising an amino acid sequence having at least 96.0% sequence identity to an amino acid sequence selected from SEQ ID NOs 1-22, preferably to SEQ ID NO: 1 ; or at least 91.0% sequence identity to an amino acid sequence selected from SEQ ID NOs 34-54, preferably to SEQ ID NO: 34.

16. Polypeptide for use in treatment, amelioration and / or prophylaxis of symptoms caused by mycotoxicosis, in particular by trichothecene mycotoxicosis, wherein the polypeptide comprises an amino acid sequence having at least 70% sequence identity to an amino acid sequence selected from SEQ ID NOs. 1-54, preferably selected from SEQ ID NOs: 1 and 34.