IL309624B2

IL309624B2 - Composition of Millard flavors and products containing them

Info

Publication number: IL309624B2
Application number: IL309624A
Authority: IL
Inventors: Gili Abramov; Daniel Dikovsky; Oded Halevi
Original assignee: Redefine Meat Ltd; Gili Abramov; Daniel Dikovsky; Oded Halevi
Priority date: 2023-12-21
Filing date: 2023-12-21
Publication date: 2025-06-01
Also published as: IL309624B1; IL309624A; WO2025134123A1

Description

0296538081- MAILLARD FLAVORING COMPOSITIONS AND PRODUCTS CONTAINING THE SAME TECHNOLOGICAL FIELD The present disclosure relates to taste and flavor compositions for the alternative food industry.

BACKGROUND ART References considered to be relevant as background to the presently disclosed subject matter are listed below: - Paulina KeRska & Joanna Stadnik "Taste-active peptides and amino acids of pork meat as components of dry-cured meat products: An in-silico study" J Sens Stud. 32:e12301. (2017) https://doi.org/10.1111/joss.123 - C. Bauchart et al. "Small peptides (<5 kDa) found in ready-to-eat beef meat" Meat Science 74:658 666 (2006) Acknowledgement of the above references herein is not to be inferred as meaning that these are in any way relevant to the patentability of the presently disclosed subject matter.

BACKGROUND The alternative meat ("alt-meat") industry is a fast-growing domain, aiming to replace livestock meat with animal-free meat homologues. A barrier in the alt-meat industry resides in the difficulty of making the alt-meat products sufficiently organoleptically similar to livestock meat. The taste and aroma (flavor) of livestock meat is typically generated during cooking via a series of thermally activated chemical reactions, most of them being classified as "Maillard Reaction". The reaction products of the Maillard reaction are also known by the term "process flavors". 0296538081- Paulina KeRska and Joanna Stadnik describe an in silico analysis of taste-active components of porcine meat for the purpose of defining the role of proteins as crucial nonvolatile components of muscle tissue and for developing a sensory profile of meat products. The publication focuses on properties of dry-cured meats and the presence of bioactive peptides released by protein hydrolysis during fermentation and aging.

C. Bauchart et al describe the postmortem occurrence of low molecular weight peptides (<5 kDa) in bovine Pectoralis profundus muscle, after storage at 4°C and vacuum cooking. Seven peptides (fragments of troponin T, nebulin, procollagen and GENERAL DESCRIPTION The present disclosure is based on the realization that while meat exudates contain thousands of peptides that may be involved in the creation of the meaty taste and aroma (typically referred to by the collective term " flavor"), only a small portion of these peptides, suffices to create Maillard flavoring sensation effect, when introduced into alternative meat products.

The present disclosure is also based on the finding that it is possible to imitate the heat induced Maillard process flavors (heat induced meaty flavor/aroma) if protein mass, suitable for use in alternative meat product, is infused with a Maillard flavoring composition comprising at least one of the peptides involved in the Maillard reaction or with functional homologues thereof, as further described herein.

Thus, in accordance with a first aspect of the presently disclosed subject matter there is provided a Maillard flavoring composition comprising at least one artificially produced peptide, wherein said at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein.

In accordance with a second aspect of the presently disclosed subject matter there is provided an alternative meat product comprising a Maillard flavoring composition according to the presently disclosed first aspect.

In accordance with a third aspect of the presently disclosed subject matter there is provided a process of producing an alternative meat product comprising infusing an 0296538081- alternative meat protein mass with a Maillard flavoring composition according to the first aspect of the presently disclosed subject matter.

BRIEF DESCRIPTION OF THE DRAWINGS In order to better understand the subject matter that is disclosed herein and to exemplify how it may be carried out in practice, embodiments will now be described, by way of non-limiting example only, with reference to the accompanying drawings, in which: Figures 1A-1B are bar graphs showing the molecular weight distribution profiles from a sirloin cut ( Figure 1A ) and from a meat chuck ( Figure 1B ).

Figures 2A-2C are a fast protein liquid chromatography chromatogram of the first injection run of sirloin exudate, for which muscle and fat tissue aggregates and protein components larger than 3 kDa were separated out ( Figure 2A) , a second injection of a lyophilized sample (resuspended in 1mL PBS buffer) of the same sirloin exudate, for which components larger than 3kDa were removed ( Figure 2B ), and an image of a sensory evaluation test conducted on each of the FPLC fractions (A to G) from the second injection (of lyophilized material) in the presence and absence of ribose ( Figure 2C ). A ribose only solution was used as a control. The fractions in this test were thermally treated.

Figures 3A-3B are bar graphs showing the molecular weight distribution profiles of peptides from fraction B ( Figure 3A ) and from fraction C ( Figure 3B ). The molecular weights of the peptides in these fractions were obtained in a proteomics analysis.

DETAILED DESCRIPTION The Maillard reaction, a pivotal process in achieving the savory and aromatic characteristics of cooked meat, presents a significant challenge in successful replication of the diverse flavor profiles and the development of artificial meat products. This chemical reaction typically occurs between amino acids and reducing sugars, resulting in the formation of melanoidins, compounds responsible for the characteristic brown color and rich flavor found in traditionally cooked meats. 0296538081- The presently disclosed subject matter aims at addressing the intricacies of the Maillard reaction in alternative meat products and offers a solution to the formidable task of reproducing the diverse and nuanced flavor compounds inherent in natural meat.

Thus, in accordance with a first aspect of the presently disclosed subject matter, there is provided a Maillard flavoring composition comprising at least one artificially produced peptide and at least one reducing sugar, wherein said at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein.

In the context of the presently disclosed subject matter, the term "hydrolysate" denotes a peptide that is obtained from hydrolysis of a naturally occurring protein where peptide bonds within the protein are cleaved, resulting in the formation of individual peptides. The hydrolysis can be by natural processes, such as enzymatic hydrolysis, and/or by chemical processes, e.g. chemical hydrolysis. Such peptide is herein referred to, at times, by the term "naturally occurring peptide".

In the context of the presently disclosed subject matter, the term "peptide" is to be understood to encompass a sequence composed of any one of the 20 naturally appearing amino acids, amino acids which have been chemically modified or composed of synthetic amino acids, as known in the art.

In the context of the presently disclosed subject matter, the term "artificially produced peptide" any peptide that is obtained by any one of hydrolysis of a non-animal protein, e.g. plant protein, recombinant expression (e.g. expression in bacteria, yeast, plant etc.), peptide synthesis (e.g. solid phase peptide synthesis (SPPS)), enzymatic synthesis and any other method known in the art for artificial production of proteins and peptides. The term "artificially produced peptide" excludes peptides that are directly extracted from an animal source, i.e. it excludes an animal exudate as the source of the peptide.

Further, in the context of the presently disclosed subject matter, the term "peptide corresponds to a hydrolysate" is to be understood to encompass a peptide that is either identical to the naturally occurring peptide that is obtained from the hydrolysis of the naturally occurring protein (i.e. the hydrolysate) or is a functional homologue of the naturally occurring peptide. 30 0296538081- In the context of the presently disclosed subject matter, the term "functional homologue" of a hydrolysate is to be understood to mean a peptide that has at least about 80% sequence identity with the hydrolysate of a naturally occurring protein, and that maintains the functionality in providing Milliard processing flavors when being part of the presently disclosed Maillard flavoring composition.

In some examples of the presently disclosed subject matter, the functional homologue has at least about 85% sequence identity with said hydrolysate of a naturally occurring protein; at times at least about 90% identity; at times, at least about 98% identity, or even at least about 99% identity with such naturally occurring peptide (obtained from the hydrolysate).

In some examples of the presently disclosed subject matter, the peptide has a sequence identical (100% identity) to the naturally occurring peptide (from the protein hydrolysate).

In some examples of the presently disclosed subject matter, the functional homologue comprises an amino acid sequence that has been subjected to any one or combination of the following, while essentially exhibiting the functionality of providing the Maillard flavoring effect in an alternative meat product: (i) one or more substitutions of an amino acid by another; (ii) one or more amino acid additions to the sequence of the naturally occurring peptide; (iii) one or more amino acid deletions from the naturally occurring peptide; and (iv) any combination of (i) to (iii).

In some examples, the amino acid sequence is subjected to at least one amino acid substitution (i.e. replacement by another amino acid).

In some examples of the presently disclosed subject matter, the substitution of at least one amino acid to form the functional homologue is a conservative substitution.

In the context of the presently disclosed subject matter, the term "conservative substitution" refers to the substitution of an amino acid in one class by an amino acid of the same class, where a class is defined by common physicochemical amino acid side chain properties and high substitution frequencies in homologous proteins found in nature, as determined, for example, by a standard Dayhoff frequency exchange matrix or BLOSUM matrix. Six general classes of amino acid side chains have been categorized and include: Class I (Cys); Class II (Ser, Thr, Pro, Ala, Gly); Class III (Asn, Asp, Gln, 0296538081- Glu); Class IV (His, Arg, Lys); Class V (Ile, Leu, Val, Met); and Class VI (Phe, Tyr, Trp). For example, substitution of an Asp for another class III residue such as Asn, Gln, or Glu, is a conservative substitution.

In the context of the presently disclosed subject matter, the term "conservative substitution" refers to the substitution of an amino acid in one class by an amino acid of the same class, where a class is defined by common physicochemical amino acid side chain properties and high substitution frequencies in homologous proteins found in nature. Classes are categorized into six general groups: Class I (Cys); Class II (Ser, Thr, Pro, Ala, Gly); Class III (Asn, Asp, Gln, Glu); Class IV (His, Arg, Lys); Class V (Ile, Leu, Val, Met); and Class VI (Phe, Tyr, Trp). For example, substitution of an Asp for another class III residue such as Asn, Gln, or Glu is considered a conservative substitution. The determination of conservative substitutions may be assessed using substitution matrices such as the BLOSUM series, which have become standard in contemporary bioinformatics, or other appropriate matrices as known in the art.

At times, the functional homologue may include one or more non-conservative substitutions as compared to the peptide hydrolysate of the naturally occurring protein, as long as the aforesaid functionality is maintained.

In the context of the presently disclosed subject matter, the term "non-conservative substitution" refers to the substitution of an amino acid in one class with an amino acid from another class; for example, substitution of an Ala, a class II residue, with a class III residue such as Asp, Asn, Glu, or Gln.

The presently disclosed Maillard flavoring composition has an effect in the alternative meat product that is sufficiently similar to the outcome of a Maillard reaction in a corresponding true meat product (i.e. the animal obtained meat product the alternative meat is aiming at imitating), by at least parameter, the at least one parameter determined by an acceptable taste panel, gas chromatography mass spectrometry (GCMS), high pressure liquid chromatography (HPLC), electronic nose, electronic tongue, EEG analysis systems (e.g. Thimus) and others, as known in the art.

In the context of the presently disclosed subject matter, the term "skeletal muscle protein" encompasses any protein that is in skeletal muscle cells, or otherwise known to be part of the skeletal muscle structure. In this context, it is to be understood that 0296538081- sarcoplasmic proteins are also proteins of the skeletal muscle, even if referred to as a separately, e.g. as a sub-group of skeletal muscle proteins.

Without being limited thereto, the skeletal muscle protein is selected from the group consisting of cysteine and glycine-rich protein 3, heat shock protein beta-6, heterogeneous nuclear ribonucleoprotein U, scaffold attachment factor A), Keratin, type I cytoskeletal 9, myomesin-1, myomesin-2, PDZ and LIM domain protein 3, RTFhomolog, Paf1/RNA polymerase II complex component, synemin, SYNPO2, nebulin, troponin I, troponin T, titin, dystrophin, myoglobin, tropomyosin, and myogenin and beta-enolase.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is nebulin.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is troponin, preferably, troponin T (fast skeletal muscle).

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is Cysteine and glycine-rich protein 3.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is Heat shock protein 6.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is Heterogeneous nuclear ribonucleoprotein U.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is Scaffold attachment factor A.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is keratin.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is type I cytoskeletal 9.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is LIM domain binding 3.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is myomesin-1. 0296538081- In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is RTF1 homolog.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is Paf1/RNA polymerase II complex component.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is SYNPO2.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is beta-enolase.

In some examples of the presently disclosed subject matter, the skeletal muscle protein comprises or is myoglobin.

In some examples of the presently disclosed subject matter, the Maillard flavoring composition comprises two or more of the at least one artificially produced peptide.

In some examples of the presently disclosed subject matter, the Maillard flavoring composition comprises two or more of the at least one artificially produced peptide that correspond to two or more peptide hydrolysates obtained from the same protein. In other words, two or more of the at least one artificially produced peptide that correspond to two or more different naturally occurring peptides obtained or derived from the same skeletal muscle protein.

In some examples of the presently disclosed subject matter, the Maillard flavoring composition comprises two or more of the at least one artificially produced peptide that correspond to two or more different hydrolysates, i.e. from different proteins. In other words, two or more of the at least one artificially produced peptide that correspond to two or more different naturally occurring peptides obtained or derived from two different proteins, at least one being the skeletal muscle protein. In some examples of the presently disclosed subject matter, the two or more different peptides are obtained from at least two, at times more than two, different skeletal muscle protein.

In some examples of the presently described subject matter, the Maillard flavoring composition comprises at least 5 different peptides of the at least one artificially produced peptide. Accordingly, the composition includes at least 5 different artificially produced peptides each corresponding to a different product of hydrolysis of the same or different proteins. 0296538081- In some examples of the presently described subject matter, the Maillard flavoring composition comprises at least 6, at times at least 7, at times, at least 8, at times, at least 9; at times, at least 10; at times, at least 11; at times, at least 12; at times, at least 13; at times, at least 14; at times, at least 15; at times, at least 16; at times, at least 17; at times, at least 18; at times, at least 19 different peptides of the at least one artificially produced peptide.

In some examples of the presently described subject matter, the Maillard flavoring composition comprises at least 10 different peptides of the at least one artificially produced peptide.

In some examples of the presently described subject matter, the Maillard flavoring composition comprises at least 15 different peptides of the at least one artificially produced peptide.

In some examples of the presently described subject matter, the Maillard flavoring composition comprises at least 20 different peptides of the at least one artificially produced peptide.

In some examples of the presently described subject matter, the Maillard flavoring composition comprises at least 25 different peptides of the at least one artificially produced peptide.

In some examples of the presently described subject matter, the Maillard flavoring composition comprises at least 30 different peptides of the at least one artificially produced peptide.

In some examples of the presently described subject matter, the Maillard flavoring composition comprises at least 35 different peptides of the at least one artificially produced peptide.

In some examples of the presently described subject matter, the Maillard flavoring composition comprises at least 39 different peptides of the at least one artificially produced peptide.

In some examples of the presently described subject matter, the Maillard flavoring composition can comprise any number falling between 5 and 39 of different peptides of the at least one artificially produced peptide. 30 0296538081- In some examples of the presently disclosed subject matter, the Maillard flavoring composition comprises at least one artificially produced peptide corresponding to a peptide hydrolysate of nebulin, and at least one other artificially produced peptide that corresponds to a peptide hydrolysate of troponin.

The artificially produced peptide(s) can have any number of amino acids between 5 and 20 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises between 7 and 18 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 5 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 6 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 7 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 8 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 9 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 10 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 11 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 12 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 13 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 14 amino acids. 0296538081- In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 15 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 16 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 17 amino acids.

In some examples of the presently disclosed subject matter, at least one of the at least one artificially produced peptide comprises 18 amino acids.

In some examples of the presently disclosed subject matter, the Maillard flavoring composition comprises at least one additional artificially produced peptide other than those corresponding to a peptide of a skeletal muscle protein.

The at least one additional artificially produced peptide can arise from different sources. Without being limited thereto, the protein source of the peptides to which the artificially produced peptides can correspond are any one of creatine kinase M-type, glyceraldehyde-3-phosphatase dehydrogenase, carbonic anhydrase 3, Phosphoglycerate kinase 1, and Synaptotagmin binding cytoplasmic RNA interacting protein.

Accordingly, in some examples of the presently disclosed subject matter, the at least one additional artificially produced peptide other than those corresponding to a peptide of a skeletal muscle protein is selected from the group consisting of creatine kinase M-type, glyceraldehyde-3-phosphatase dehydrogenase, carbonic anhydrase 3, Phosphoglycerate kinase 1, and Synaptotagmin binding cytoplasmic RNA interacting protein.

In some examples of the presently disclosed subject matter, the at least one additional artificially produced peptide corresponds to a hydrolysate peptide of creatine kinase.

In some examples of the presently disclosed subject matter, the at least one additional artificially produced peptide corresponds to a hydrolysate peptide of glyceraldehyde-3-phosphatase dehydrogenase. 0296538081- In some examples of the presently disclosed subject matter, the at least one additional artificially produced peptide corresponds to a hydrolysate peptide of carbonic anhydrase 3.

In some examples of the presently disclosed subject matter, the at least one additional artificially produced peptide corresponds to a hydrolysate peptide of Phosphoglycerate kinase 1.

In some examples of the presently disclosed subject matter, the at least one additional artificially produced peptide corresponds to a hydrolysate peptide of Synaptotagmin binding cytoplasmic RNA interacting protein.

In some examples of the presently disclosed subject matter, the at least one artificially produced peptide or the at least one additional artificially produced peptide is a peptide selected from the peptides listed in Tables 1A-1B and any functional homologue of same.

Table 1A: Artificially Produced Peptides Corresponding To Peptides From Skeletal Muscle Peptide Source Sequence Length SEQ ID NO.

Cysteine and glycine-rich protein PNWGGGAK 8 Heat shock protein 6 VPVQPSW 7 Heterogeneous nuclear ribonucleoprotein U, Scaffold attachment factor A GQFWGQKP 8 Keratin, type I cytoskeletal SRSGGGGGGGLGSGGSIRSSY LIM domain binding 3 SDFSGSLPIKD 11 LIM domain binding 3 SGSLPIKD 8 Myomesin-1 YDYGYSH 7 Myomesin-1 YDYGYSHG 8 Nebulin DAIPITAAKASRN 13 Nebulin DEYNHFFK 8 Nebulin DNIYKHDW 8 11 0296538081- Nebulin DSHYKADW 8 Nebulin QPIHHYTY 8 Nebulin SDNIYKHDW 9 Nebulin SEYKYKEGFR 10 Nebulin TPEIIHAQQVKN 12 PDZ and LIM domain protein TPSGVDGGSGRSTP 14 RTF1 homolog, Paf1/RNA polymerase II complex component HDFDVKI 7 Synemin EENEGHWF 8 SYNPO2 LPAGWKY 7 SYNPO2 LPAGWKYS 8 Troponin T, fast skeletal muscle APPPPAEVPEVHEEVH 16 Troponin T, fast skeletal muscle EAPPPPAEVPEVHEEVH Troponin T, fast skeletal muscle EEAPPPPAEVPEVHEEVH Troponin T, fast skeletal muscle VPEVHEEVH 9 Table 1B Artificially Produced Peptides Corresponding To Peptides From Sarcoplasmic Reticulum (SR) Peptide Source Sequence Length SEQ ID NO.Carbonic anhydrase 3 AKEWGYADHN 10 Creatine kinase M-type DEESYTVFKD 10 Creatine kinase M-type EFKGKYY 7 Creatine kinase M-type GDEESYTVFKD 11 Creatine kinase M-type GEFKGKYY 8 Creatine kinase M-type GEFKGKYYP 9 31 0296538081- Creatine kinase M-type TGEFKGKYY 9 Creatine kinase M-type TGEFKGKYYP 10 Glyceraldehyde-3-phosphate dehydrogenase DNEFGYSNR 9 Glyceraldehyde-3-phosphate dehydrogenase NDHFVKL 7 Glyceraldehyde-3-phosphate dehydrogenase NEFGYSNR 8 Glyceraldehyde-3-phosphate dehydrogenase YDNEFGYSNR 10 Phosphoglycerate kinase 1 EGKVLPGVDA 10 Synaptotagmin binding cytoplasmic RNA interacting protein DDYYYYGPPH 10 In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:1.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:2.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:3.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:4.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:5.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:6.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO: 7. 15 0296538081- In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:8.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:9.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:10.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:11.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:12.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:13.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:14.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:15.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:16.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:17.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:18.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:19.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:20.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:21. 0296538081- In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:22.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:23.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:24.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:25.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:26.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:27.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:28.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:29.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:30.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:31.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:32.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:33.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:34.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:35. 0296538081- In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:36.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:37.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:38.

In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of SEQ ID NO:39.

The Maillard flavoring composition also comprises at least one reducing sugar.

In the context of the presently disclosed subject matter, when referring to a "reducing sugar" it is to be understood to have its regular, commonly acceptable meaning in the art. Yet, for the sake of clarity, it should be understood to encompass any carbohydrate compound possessing a free aldehyde or ketone functional group that is capable of reducing another compound (the property can be determined by its ability to react with reagents such as Fehling's solution or Benedict's solution).

In some examples of the presently disclosed subject matter, the at least one reducing sugar comprises or is a saccharide containing molecule.

In some examples of the presently disclosed subject matter, the at least one reducing sugar comprises or is a monosaccharide. A non limiting list of monosaccharides includes glucose, fructose, galactose, ribose, glyceraldehyde and xylose.

In some examples of the presently disclosed subject matter, the at least one reducing sugar comprises or is a disaccharide. A non limiting list of disaccharides includes maltose, cellobiose and lactose.

In some examples of the presently disclosed subject matter, the at least one reducing sugar comprises a combination of at least one monosaccharide and at least one disaccharide.

In some examples of the presently disclosed subject matter, the composition comprises two or more reducing sugars.

In some examples of the presently disclosed subject matter, the at least one reducing sugar comprises at least ribose. 30 0296538081- The Maillard flavoring composition also comprises at least one amino acid monomer.

In the context of the presently disclosed subject matter, when referring to an "amino acid monomer" it is to be understood to include any compound including an amino group, a carboxyl group and a side chain. The amino acid monomer can be a naturally occurring amino acid, a synthetic or a modified amino acid monomer (e.g. a naturally occurring amino acid that has been chemically modified), all as known in the art.

In some examples, the amino acid monomer is any one of the 20 naturally occurring monomers, i.e. any one of Alanine (Ala, A), Cysteine (Cys, C), Aspartic acid (Asp, D), Glutamic acid (Glu, E), Phenylalanine (Phe, F), Glycine (Gly, G), Histidine (His, H), Isoleucine (Ile, I), Leucine (Leu, L), Lysine (Lys, K), Methionine (Met, M), Asparagine (Asn, N), Glutamine (Gln, Q), Proline (Pro, P), Arginine (Arg, R), Serine (Ser, S), Threonine (Thr, T), Tryptophan (Trp, W) and Tyrosine (Tyr, Y), as well as derivatives of naturally occurring amino acids, such as, without being limited thereto, taurine, ornithine, cystine, citrulline.

In some examples of the presently disclosed subject matter, the amino acid monomer is selected from glutathione, taurine, ornithine, carnosine, cystine, citrulline, -and alanine.

Without being bound thereto, it has been now found that adding free amino acid monomers, such as those listed above, boost the meaty flavor and aroma, preferably when combined with said at least one reducing sugar. Table 2 provides a non-limiting example of relative amounts of amino acids (range out of total amount of free amino acid and suggested specific relative amount (±0.1) out of total amount of free amino acid) that may be present in the Maillard flavoring composition of the presently disclosed subject matter. In the context of the presently disclosed subject matter, the described range or suggested specific % for each free amino acid constitutes a separate example of the presently disclosed subject matter, and further, any combination of two or more of the amino acids listed in Table 2 including their ranges or relative amount.

Table 2: Free Amino Acid Relative Amounts Amino acid % range free amino acids % out of total free amino acids 0296538081- Ala 18-22 19.Arg 0.5-1.5 1.Asn 0.7-1.7 1.Asp 0.05-0.5 0.Gln 12-18 15.Glu 1-5 2.Gly 5-10 7.His 0.5-1.5 0.Ile 1.5-4 2.Leu 10-15 12.Lys 2-6 4.Met 0.5-1.5 0.Phe 3-6 4.Pro 3-6 4.Ser 1.5-4 2.Thr 1-4 2.Trp 0.1-1 0.Tyr 3-6 4.Val 1.5-4 2.D-ribose 8-12 The Maillard flavoring composition can be provided in any physical form, including dry, semi-dry/semi-liquid, and liquid form.

In some examples of the presently disclosed subject matter, the Maillard flavoring composition is in dry form, this includes, without being limited thereto, dehydrated or lyophilized.

In some examples of the presently disclosed subject matter, the Maillard flavoring composition is in semi-dried form, e.g. paste like form.

In some examples of the presently disclosed subject matter, the Maillard flavoring composition is animal-free. 10 0296538081- In the context of the presently disclosed subject matter, when referring to an "animal free" composition or product it is to be understood that at least the at least one peptide in the Maillard flavoring composition is not derived or obtained from an animal source, e.g. from an exudate of animal part.

In some examples of the presently disclosed subject matter, the Maillard flavoring composition is absence of any component or ingredient that was obtained or derived from animal source.

The Maillard flavoring composition is preferably for use in providing a flavor or aroma to alternative meat products once the alternative meat product having the composition is heated, e.g. cooked, fried, backed, roasted, grilled, pan-seared, broiled, barbecued. It has been found that the presently disclosed Maillard flavoring composition is effective to provide the desired flavor (taste and aroma) that would be ranked by a taste panel as an acceptable imitation of the Maillard reaction taking place in the corresponding true meat, heated under same or similar conditions. For example, a Maillard flavoring composition according to the presently disclosed subject matter designed for an alternative Sirloin meat product would provide the alternative Sirloin meat product with taste and aroma similar to a true Sirloin cut.

In line with the above, the presently disclosed subject matter also provides, in accordance with a second of its aspects, an alternative meat product comprising the presently disclosed Maillard flavoring composition.

For simplicity, all definitions and terms used with respect to the presently disclosed Maillard flavoring composition also apply to the presently disclosed alternative meat product.

The alternative meat product disclosed herein can be of any type and form.

In some examples of the presently disclosed subject matter, the alternative meat product is an alternative whole muscle cut.

In some examples of the presently disclosed subject matter, the alternative meat product is an alternative minced meat.

The alternative meat product according to the presently disclosed subject matter, comprises protein(s) mass in combination with the presently disclosed Maillard flavoring composition. 0296538081- In some examples of the presently disclosed subject matter, the protein(s) comprise plant proteins. The plant proteins can be in the form of a pure protein, a protein isolate, protein concentrate, protein flour, texturized protein such as texturized vegetable protein (TVP).

In the context of the present disclosure, TVP is used to denote both dry form of texturized vegetable protein (sometimes regarded to as expanded TVP), as well as high moisture form, known in the art as the outcome of high moisture extrusion (HME) or high moisture extrusion cooking (HMEC) or similarly. TVP may also denote any TVP and/or the degree of expansion of the TVP is intermediate between those typically found in dry (expanded) form and HME(C) form.

The protein(s) of the protein mass can be of any plant source, this includes, without being limited thereto, wheat, legume (pulses, beans, peas, lentils, nuts), plant seeds and grains (e.g. sunflower, canola, rice), stem or tuber protein (e.g. potato protein).

In some examples of the presently disclosed subject matter, the proteins of the protein(s) mass are derived from legume. Specific, yet non-limiting examples of legume/bean proteins include, soy protein, pea protein, chickpea protein, lupine protein, mung-bean protein, kidney bean protein, black bean protein, alfalfa protein.

The protein of the protein(s) mass may include a single type of protein or a blend of proteins.

In some examples of the presently disclosed subject matter, at least some of the proteins of the protein mass contain a recombinant protein, derived from e.g. plants, algae, fungi, and/or microorganisms.

The protein mass can include edible additives, such as, without being limited thereto, fibers originating from either protein and/or carbohydrate origin, including without limitation starches and dietary nutritional fibers (and other forms of cellulose-based fibers); colorants (e.g. annatto extract, caramel, elderberry extract, lycopene, paprika, turmeric, spirulina extract, carotenoids, chlorophyllin, anthocyanins, and betanin), emulsifiers, acidulants (e.g. vinegar, lactic acid, citric acid, tartaric acid malic acid, and fumaric acid), flavoring agents or flavoring enhancing agents (e.g. monosodium glutamate), antioxidants (e.g. ascorbic acid, rosemary extract, aspalathin, quercetin, and 0296538081- various tocopherols), dietary fortifying agents (e.g. amino acids, vitamins and minerals), preservatives, stabilizers, sweeteners, gelling agents, thickeners and dietary fibers (e.g. fibers originating from citrus source).

The protein mass is infused (e.g. marinated) with the Maillard flavoring composition. The infusion can be to an extend that the Maillard flavoring composition penetrates into the protein mass, or at least into portions of the protein mass.

As used herein, the term "infused" denotes the process by which the flavoring composition permeates and becomes incorporated into the protein mass of the meat alternative. The infusion involves the introduction of the Maillard flavoring composition into the protein matrix, allowing for the absorption and integration of flavor constituents, thereby enhancing the overall sensory characteristics of the meat alternative. The infusion may occur through methods such as marination, soaking, or any other suitable technique that facilitates the uniform distribution of the flavoring composition within the protein mass.

In some examples of the presently disclosed subject matter, the protein mass of the alternative meat product is constructed as a muscle scaffold/protein matrix.

The presently disclosed subject matter, also provides, in accordance with a third of its aspects, a process of producing an alternative meat product. The process comprises infusing an alterative meat protein mass with a Maillard flavoring composition as presently disclosed.

The infusion, as described above, is the process by which the presently disclosed Maillard flavoring composition permeates and becomes incorporated into the protein mass of the meat alternative.

The infusion may occur through methods such as marination, soaking, or any other suitable technique that facilitates the uniform distribution of the flavoring composition within the protein mass.

As used herein in the specification and in the claim, the forms "a", "an" and "the" include singular as well as plural references unless the context clearly dictates otherwise. For example, the term "a protein " includes one or more proteins.

As used herein in the specification and in the claim, the form and/or either or both 0296538081- conjunctively present in some cases and disjunctively present in other cases. Multiple and/or one or moreof the elements so conjoined.

Further, as used herein, the term "comprising" is intended to mean that a recited element, e.g. Maillard flavoring compositon, includes the recited components, e.g. artificially produced protein and reducing sugar, but not excluding other elements, such as amino acids. The term "consisting essentially of" is used to define elements which include the recited components but exclude other components that may have an essential significance on the functionality of the element. "Consisting of" shall thus mean excluding more than trace amounts of other componnts in an element. Embodiments defined by each of these transition terms are within the scope of this invention.

Further, as used herein, the term "essentially" or "generally" or "substantially" is intended to mean that a defined property or element can have 10% deviation from the recited value.

Further, as used herein, the term "about" is intended to mean that all numerical values, e.g. amounts or ranges, are approximations which are varied (+) or (-) by up to 20%, at times by up to 10% of from the stated values.

The invention will now be exemplified in the following description of experiments that were carried out in accordance with the invention. It is to be understood that these examples are intended to be in the nature of illustration rather than of limitation. Obviously, many modifications and variations of these examples are possible in light of the above teaching. It is therefore, to be understood that within the scope of the appended claims, the invention may be practiced otherwise, in a myriad of possible ways, than as specifically described hereinbelow.

DESCRIPTION OF NON-LIMITING EXAMPLES In the following non-limiting examples, the following equipment was used: Ultrafiltration was performed using Amicon® Ultra-15 Centrifugal-Filter Unit devices (Ultracel® regenerated cellulose membrane with either a 10kDa or 3kDa cutoff).

Gel filtration was performed using Sephadex G-25 resin (Cytiva). 0296538081- Solid phase extraction was performed using Oasis HLB reversed-phase sorbent (Waters) and Oasis MCX mixed-mode cationic sorbent (Waters).

Liquid chromatography mass spectrometry (LC-MS) - was performed using nanoflow liquid chromatography (nanoAcquity) coupled to high resolution, high mass accuracy mass spectrometry (Q Exactive Plus).

Data Analysis Raw data was processed with MetaMorpheus version 0.0.320. The data was searched against the bovine proteome database appended with common lab protein contaminants. Quantification was performed using the embedded FlashLFQ and protein inference algorithms. It is noted that quantitative information for each peptide in a sample was not absolute, but rather comparative when more than one sample is being analyzed.

Size-exclusion fast protein liquid chromatography (FPLC) was performed using AKTA pureTM protein purification system equipped with Superdex 30 Increase column, suitable for the purification and analysis of peptides in the range 100-7000 Da to.

Measurement of peptides concentrations was performed using NanoDropTM OneC Microvolume UV-Vis spectrophotometer.

Gas Chromatography Mass Spectroscopy (GC-MS) - was performed using headspace solid-phase microextraction (HS-SPME) sampling technique, coupled to a Gerstel MultiPurpose PAL sampler (MPS) fitted with a 120 m Divinylbenzene /Polydimethylsiloxane (DVB /PDMS) SPME arrow fiber (CTC analytics, Zwingen, Switzerland). Extracted compounds were subsequently separated and analyzed using an Agilent 7890B/5977B GC-MS system equipped with an Agilent HP-5ms capillary column (30 m x 0.25 mm x 0.25 m).

Example 1: Peptides extraction and characterization Peptides were extracted from livestock meat products and characterized by reverse-engineering their flavor generating mechanisms and outlining the specific molecules and molecular profiles that has major contribution to cooked meat flavors.

Specifically, meat exudate (ME) was collected from different raw beef meat cuts via vacuuming small chunks of the meat and storing at 5°C for a period of up to 3 days. The meat exudate was separated from the meat and stored at -20°C until further analysis. 30 0296538081- To identify the peptides in the MJ, the following experiments and analyses were performed: Peptidomics: LC-MS analysis Two MJ were obtained and analyzed by LC-MS, one from sirloin and anoterh from chunk and were applied to Amicon® ultrafiltration devices with a 10 kDa molecular cutoff so as to separate peptides (and amino acids) having a MW below 10kDa from other (larger than 10kDa) components in the MJ.

The obtained peptides fractions were separately subjected to Sephadex 25 gel filtration (for buffer exchange and removal of contaminants) and MCX (mixed-mode cationic exchange) solid phase extraction (a standard step of purification prior to the chromatographic analysis).

The resulting purified peptides were analyzed via liquid chromatography mass spectrometry (LC-MS) to reveal their molecular composition. Each sample was analyzed on the instrument separately in a random order in discovery mode.

From the two samples, a total of 9,221 different peptides were identified: 8,465 peptides from the sirloin cut and 8,829 from meat chuck.

The molecular weight distributions of the MJ peptides from the sirloin cut and from the meat chuck are provided in Figures 1A and 1B , respectively.

Figures 1A-1B show that the molecular weight distribution profile was similar in both cuts and centered around a mass of ~1500 Da. A comparison between the sequences of the two cuts showed there is 88% overlap between the peptides from both cuts, that is, 88% of all peptides are identical in sequence and size in both cuts. This was determined using Peptidomics analysis. Generally, Peptidomics analysis gives lists of peptides and their relative intensity. To identify the overlap, each peptide was identified by its relative intensity (if a peptide was present, it was assigned with a non-zero intensity value while if a peptide was absent, it was assigned a zero-intensity). The number of peptides that had a non-zero intensity in both sirloin and chuck was determined and divided by the total number of peptides. 0296538081- Sample preparation and size-exclusion fast protein liquid chromatography (FPLC) To identify the specific peptides that contribute to the aroma profile of cooked meat, a subsequent analysis of sirloin MJ was performed using size-exclusion liquid chromatography. The rationale behind running FPLC was to narrow down the many different sequences of peptides to several pools of peptides, each with a certain molecular weight range.

Specifically, MJ was centrifuged extensively by ultracentrifugation (400,000 g) to remove solids and aggregates. The supernatant was filtered using a 0.45 m and then centrifuged using Amicon® ultrafiltration devices with a 3 kDa molecular cutoff, yielding the final clear liquid phase in the flow-through.

A sample of the clear liquid phase was subjected to FPLC. The first run was of 1ml of the clear liquid phase described above, injected onto a Superdex 30 Increase column (equilibrated with PBS buffer) (see in this connection Figure 2A). The rest of the purified/ clear liquid phase sample (i.e., prior to FPLC run) was lyophilized and resuspended in a 1mL PBS to be used as a single second injection (see in this connection Figure 2B).

The flow rate was 1 mL/min, and the column (Superdex 30) bed volume is about 24mL (the separation range of this column is typically between 100-7000 Da).

Figure 2A provides fast protein liquid chromatography chromatogram showing protein absorbance at 280 nm as a function of the elution volume of the first injection performed on the sirloin MJ (for which muscle and fat tissue aggregates and protein components larger than 3 kDa were separated out). The chromatogram presents different peaks, identified as peaks A, B, C, D, E, F, G, as further discusses below.

Figure 2B is the chromatogram of the second injection. The same running conditions were used for the first and second injection. The second injection is of a sample that is much more concentrated than the first injection, and therefore some of the fractions, e.g., B and C are less resolved. The same fraction volumes were collected for both injections. 0296538081- Sensory test of FPLC-isolated fractions The six fractions, identified as fractions A, B, C, D, E, F, G were collected from the FPLC run described above for the sirloin MJ. 100 L and 50uL of each of the A to G fractions were placed on a thin glass plate and heated at 175°C, in the absence and in the presence of D-ribose at a 1:1 ratio, respectively. D-ribose alone was also heated under the same experimental setup for control.

Figure 2C depicts the result of these experiments for each of the fractions from Figure 2B. "Ribose (R)" represents the control experiment where no browning was observed. "Peptides (P)" represents the heating of each fraction in the absence of ribose, and "P+R" represents the heating of each fraction in the presence of ribose. Browning was observed for fractions B and C and is indicative of the Maillard reaction. A Typical meaty aroma accompanied the browning (based on a sensory panel). No significant difference in the aroma was reported between fractions B and C. The sensory experiment confirmed that the peptides in fractions B and C can react in the Maillard reaction and generate the desired meaty aroma.

The fractions concentrations were measured using the Nanodrop and the A2method, in which an extinction coefficient of 31 mL mg-1cm-1 is being used, to compensate for lack of Trp or Tyr residues that contribute to A280 of proteins. The measurement was conducted as described by Scopes, RK [Scopes, RK "Measurement of protein by spectrophotometry a 205 nm" Analytical Biochemistry. 59:277-282 (1974)].

Fractions B, C, D, E, F and G were sent to Peptidomics. Fraction B contained 1139 different peptides, fraction C contained 39 peptides, and all the other fractions contained few peptides only. The molecular weight distribution of the peptides in fractions B and C is given in Figure 3A and Figure 3B , respectively, showing that most of the peptides have a molecular weight between 900 and 1700Da in fraction B and between 800 and 1300Da in fraction C.

Table 3 provides a list of 39 peptides that contribute to Maillard reaction and meat process flavor, as determined using Peptidomics of FPLC fractions. 0296538081- Table 3 Selected peptides as meat process flavors Peptide Sequence No of amino acids SEQ ID NO: AKEWGYADHN 10 APPPPAEVPEVHEEVH 16 DAIPITAAKASRN 13 DDYYYYGPPH 10 DEESYTVFKD 10 DEYNHFFK 8 DNEFGYSNR 9 DNIYKHDW 8 DSHYKADW 8 EAPPPPAEVPEVHEEVH 17 EEAPPPPAEVPEVHEEVH 18 EENEGHWF 8 EFKGKYY 7 EGKVLPGVDA 10 GDEESYTVFKD 11 GEFKGKYY 8 GEFKGKYYP 9 GQFWGQKP 8 HDFDVKI 7 LPAGWKY 7 LPAGWKYS 8 NDHFVKL 7 NEFGYSNR 8 36 0296538081- Peptide Sequence No of amino acids SEQ ID NO: PNWGGGAK 8 QPIHHYTY 8 SDFSGSLPIKD 11 SDNIYKHDW 9 SEYKYKEGFR 10 SGSLPIKD 8 SRSGGGGGGGLGSGGSIRSSY 21 TGEFKGKYY 9 TGEFKGKYYP 10 TPEIIHAQQVKN 12 TPSGVDGGSGRSTP 14 VPEVHEEVH 9 VPVQPSW 7 YDNEFGYSNR 10 YDYGYSH 7 YDYGYSHG 8 Properties of the peptides in fractions B and C Peptides fractions B and C from the FPLC above were collected and sent for Peptidomics. The latter analysis revealed that fraction B contained a total of 1139 peptides and fraction C contained 39 peptides in total. For each peptide, the amino acids sequence was provided, giving also each peptide's molecular weight, as well as the protein from which this peptide originated.

Fractions B and C were selected as the fractions with the highest potential to generate basic aroma of cooked beef, as evident from Figure 2C . 0296538081- Fractions B and C contained 1139 and 39 peptides, respectively. The peptides in fraction C correspond to 17 protein types as listed in Tables 1A and 1B, the data being based on Peptidomics analysis. Ten of these proteins contribute a single peptide to fraction C. Most of the other peptides originate from 4 protein types, including the myofibrillar proteins nebulin and troponin and the sarcoplasmic proteins creatine kinase and glyceraldehyde-3-phosphatase dehydrogenase. The latter are enzymatic proteins that are abundantly found in the sarcoplasm. These same 4 proteins are also the most abundant proteins that produce the peptides in fraction B. In both fractions the peptides count is highest for nebulin.

Both fractions produce a similar aroma profile upon cooking, and both have overlapping peptide sequences. 69% of the peptides in fraction C are also present in fraction B (100% identity) with either lower or comparable intensity. 82% of peptides in fraction B are either identical or similar in sequence, that is the peptide's origin is from the same protein as in B but with 1 or up to 3 amino acids removed at the terminal. The average molecular weight of the peptides in fraction C is 1148 Da and the average length is 10 amino acids.

Amino acids composition in fraction C peptides: none of the peptides in fraction C contained cysteine and methionine. Glycine was the most abundant amino acid, followed by proline, glutamic acid and glutamine, and lysine.

Gas Chromatography Mass Spectroscopy (GC-MS) analysis Furthermore, the meat exudate was separated into fractions and analyzed for its process flavors and specifically for meaty aroma, using GC-MS.

The fractions will be separated and formulated to mimic simplified alt-meat samples and then cooked, while collecting the volatiles. The volatiles/odorants will be analyzed sensorially and also using the olfactory feature in GCMS.

Claims

- 31 - 309624/ 02965380145- CLAIMS:

1. A composition comprising at least one artificially produced peptide and at least one reducing sugar, wherein said at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein; wherein said composition is for use in combination of food; and wherein upon heating of said combination, said composition provides a Maillard reaction in said food.

2. The composition of claim 1, comprising two or more of said at least one artificially produced peptide.

3. The composition of claim 2, wherein said two or more of said at least one artificially produced peptide correspond to two or more hydrolysates of a same skeletal muscle protein.

4. The composition of claim 2, wherein said two or more of said at least one artificially produced peptide correspond to two or more hydrolysates of two different skeletal muscle protein.

5. The composition of any one of claims 1 to 4, comprising at least 5 of said at least one artificially produced peptide.

6. The composition of any one of claims 1 to 5, wherein skeletal muscle protein is selected from the group consisting of cysteine and glycine-rich protein 3, heat shock protein beta-6, heterogeneous nuclear ribonucleoprotein U, scaffold attachment factor A), Keratin, type I cytoskeletal 9, myomesin-1, myomesin-2, PDZ and LIM domain protein 3, RTF1 homolog, Paf1/RNA polymerase II complex component, synemin, SYNPO2, nebulin, troponin I, troponin T, titin, dystrophin,, tropomyosin, myogenin, beta-enolase and myoglobin.

7. The composition of any one of claims 1 to 6, wherein said skeletal muscle protein is nebulin. - 32 - 309624/ 02965380145-

8. The composition of any one of claims 1 to 6, wherein said skeletal muscle protein is troponin.

9. The composition of claim 7 or 8, comprising at least one artificially produced peptide that corresponds to a hydrolysate of nebulin, and at least one artificially produced peptide that corresponds to a hydrolysate of troponin.

10. The composition of any one of claims 1 to 9, wherein said at least one artificially produced peptide is a hydrolysate of the skeletal muscle protein or a functional homologue of a hydrolysate of the skeletal muscle protein.

11. The composition of any one of claims 1 to 10, wherein said at least one artificially produced peptide comprises between 5 and 20 amino acids.

12. The composition of any one of claims 1 to 11, wherein said at least one artificially produced peptide comprises between 7 and 18 amino acids.

13. The composition of any one of claims 1 to 12, comprising at least one additional artificially produced peptide that corresponds to a hydrolysate of a protein selected from the group consisting of creatine kinase M-type, glyceraldehyde-3-phosphatase dehydrogenase, carbonic anhydrase 3, Phosphoglycerate kinase 1, and Synaptotagmin binding cytoplasmic RNA interacting protein.

14. The composition of any one of claims 1 to 13, comprising at least one artificially produced peptide comprises or consists of an amino acid sequence designated by any one of SEQ ID NO:1 to SEQ ID NO:25 and any functional homologue of same.

15. The composition of claim 13, wherein said at least one additional artificially produced peptide comprises or consists of an amino acid sequence designated by any one of SEQ ID NO: 26 to SEQ ID NO:39 and any functional homologue of same.

16. The composition of any one of claims 1 to 15, comprising between about 5 and of said at least one artificially produced peptides.

17. The composition of any one of claims 1 to 16, wherein said at least one reducing sugar is selected from the group consisting of glucose, glucose-6 phosphate, galactose, fructose, ribose, maltose, glyceraldehyde, xylose, cellobiose, lactose. - 33 - 309624/ 02965380145-

18. The composition of any one of claims 1 to 17, wherein said at least one reducing sugar comprises at least ribose.

19. The composition of any one of claims 1 to 18, comprising two or more reducing sugars.

20. The composition of any one of claims 1 to 19, comprising at least one amino acid monomer.

21. The composition of any one of claims 1 to 20, in dry form.

22. The composition of any one of claims 1 to 21, being animal-free.

23. An alternative meat product comprising a composition as claimed in any one of claims 1 to 22.

24. The alternative meat product of claim 23, comprising an alternative meat protein mass infused with said composition.

25. The alternative meat product of claim 24, wherein said alternative meat protein mass is in a form of a muscle scaffold.

26. A process of producing an alternative meat product comprising infusing an alternative meat protein mass with a composition as claimed in any one of claims 1 to 22.