Compositions for aromatization comprising maillard precursors and products containing the same

Abstract

he present disclosure provides A composition comprising at least one artificially produced peptide and at least one reducing sugar for use with edible protein mass, as an alternative meat product. The at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein. Upon heating the composition, after infusion into an edible protein mass, a Maillard reaction occurs within the edible protein mass. Also disclosed is an alternative meat product comprising an edible protein mass infused with the disclosed composition, and method of producing the alternative meat product.

Description

[0001] COMPOSITIONS FOR AROMATIZATION COMPRISING MAILLARD PRECURSORS AND PRODUCTS CONTAINING THE SAME

[0002] TECHNOLOGICAL FIELD

[0003] The present disclosure relates to taste and flavor compositions for the alternative food industry.

[0004] BACKGROUND ART

[0005] References considered to be relevant as background to the presently disclosed subject matter are listed below:

[0006] Sohail A. et al. “Aroma compounds identified in cooled meat: A review” Food Research International 157 111385 (2022)

[0007] 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:el2301. (2017) https: / / doi.org / 10. i n i / ios .12301

[0008] C. Bauchart. et al. "Small peptides (<5 kDa) found in ready-to-eat beef meat" Meat Science 74:658-666 (2006)

[0009] International patent application publication No. WO2018185318

[0010] 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.

[0011] BACKGROUND

[0012] 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 odorants and also known by the term "process flavors". Such odorants are discussed by Sohail A et al.

[0013] 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.

[0014] 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 cypher proteins) were identified in cooked meat extracts.

[0015] WO2018185318 describes a flavor modifier composition for a meat analog. The flavor modifier composition includes a yeast extract; a fatty acid; peptide material having a molecular weight of from about 300 to about lO.OOODa; and at least two free amino acids wherein at least one free amino acid is a sulfur containing amino acid.

[0016] GENERAL DESCRIPTION

[0017] The present disclosure is based on the inventors’ 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 (less than 100) of these peptides, suffices to create Maillard flavoring reaction and as a result a Maillard flavoring sensation effect, when introduced into protein mass that is suitable for providing alternative meat products. This realization is different from the scenario where compositions already providing a Maillard sensation are introduced as is into an alternative meat protein.

[0018] The present disclosure is also based on the inventors’ finding that it is possible to imitate a heat-induced, Maillard process flavors (heat induced meaty flavor / aroma) if protein mass, suitable for use in alternative meat product (which is referred to at times as the protein matrix), is infused with a composition comprising artificially produced peptides that were identified by the inventors of the present invention to be effective to provide a Maillard reaction once heated with the protein mass, as further described herein.

[0019] Further, the present disclosure is based on the realization that even an arbitrary selection of peptides that are hydrolysates of skeletal muscle protein, effectively provided Maillard reaction and Maillard volatiles. This led to the conclusion that any artificially produced peptide that corresponds to hydrolysate and that produces same volatiles upon heating with a protein mass, as further described herein, would be suitable for use according to the present disclosure.

[0020] As detailed below, the artificially produced peptides are specifically selected to allow the occurrence of the Maillard reaction once heated with the protein mass, and these specifically correspond to a hydrolysate of skeletal muscle protein.

[0021] Thus, in accordance with its broadest scope, the presently disclosed subject matter there is provided a composition comprising at least one artificially produced peptide, wherein said at least one artificially produced peptide corresponds to a hydrolysate of meat juice proteins.

[0022] The meat juice proteins are the proteins that exist in liquids extracted from meat, and this includes preferably, at least skeletal muscle protein.

[0023] The first disclosed aspect, thus relates to a composition comprising at least one artificially produced peptide, wherein said at least one artificially produced peptide corresponds to a hydrolysate of at least one skeletal muscle protein.

[0024] An advantage of the composition comprising the at least one artificially produced peptide is that upon heating the composition after infusion into an edible protein mass, a Maillard reaction occurs within the edible protein mass.

[0025] In the context of the presently disclosed aspects, is to be understood that the disclosed composition provides the edible protein mass with meaty flavor and / or meaty aroma and / or volatiles derived from meat, upon heating the edible protein mass infused with the disclosed composition, and that these meaty flavor and / or meaty aromas and / or volatiles derived from meat are absent from the composition prior to heating.

[0026] In some examples of the present disclosure, the disclosed composition does not possess any meaty volatiles prior to heating. Further, in accordance with a second aspect of the presently disclosed subject matter there is provided an alternative meat product comprising an edible protein mass infused with a composition comprising at least one reducing sugar and at least one artificially produced peptide, wherein said at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein. Upon heating the composition, after being infused into the edible protein mass, a Maillard reaction occurs within the edible protein mass. It has been found that there is an advantage in the alternative meat product’s organoleptic properties, when produced from edible mass infused with the disclosed composition over products that are infused with Maillard process flavors prior to heating.

[0027] It is to be understood that the term “Maillard process flavors” refers to the complex and distinctive volatiles that result from the Maillard reaction, namely, the chemical reaction between amino acids and reducing sugars that occurs when food is heated, typically above 140°C (284°F).

[0028] Yet, in accordance with a third aspect of the presently disclosed subject matter there is provided a process of producing an alternative meat product, the process comprises infusing an edible protein mass with a composition comprising at least one reducing sugar and at least one artificially produced peptide, wherein the at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein. The composition is suitable for creating a Maillard reaction within the edible protein mass, upon heating the composition, after being infused into an edible protein mass, a Maillard reaction occurs within the edible protein mass .

[0029] BRIEF DESCRIPTION OF THE DRAWINGS

[0030] 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:

[0031] Figures 1A-1B are bar graphs showing the molecular weight distribution profiles of hydrolysates of skeletal muscle protein from a sirloin cut (Figure 1A) and from a meat chuck (Figure IB). Figures 2A-2C are a fast protein liquid chromatography (FPLC) chromatograms 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 ImL 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 (fractions “A” to “G”, as described below) 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 at 175°C.

[0032] Figures 3A-3B are bar graphs showing the molecular weight distribution profiles of peptides from fraction B of Figure 2B (peptides have a molecular weight between 900 and 1700Da, Figure 3A) and from fraction C of Figure 2B (peptides having a molecular weight between 800 and 1300Da, Figure 3B). The molecular weights of the peptides in these fractions were obtained in a proteomics analysis.

[0033] Figure 4 is GC-MS chromatograms of cooked and of uncooked / raw Ribeye beef loin.

[0034] DETAILED DESCRIPTION

[0035] 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.

[0036] 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 to Maillard reaction in natural, animal meat.

[0037] Thus, in accordance with a first aspect of the presently disclosed subject matter, there is provided a composition comprising at least one artificially produced peptide and at least one reducing sugar, wherein the at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein. The composition has the advantage of providing a Maillard reaction within the edible protein mass, once infused into and heated with the protein mass.

[0038] In the context of the presently disclosed first, second and / or third aspects, the term "hydrolysate" refers to a sequence of 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 providing the hydrolysate can be by natural processes, such as enzymatic hydrolysis, and / or by chemical processes, e.g. chemical hydrolysis. In the context of the present disclosure, the hydrolysate is an artificially produced peptide that has an amino acid sequence corresponding to that of a peptide produced by such hydrolysis from the naturally occurring protein. The naturally produced peptide (i.e. the product of hydrolysis of the naturally occurring protein) is herein referred to, at times, by the term "naturally occurring peptide" .

[0039] In the context of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the term "artificially produced 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.

[0040] Further, in the context of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the term "artificially produced peptide" denotes any sequence of amino acids that correspond with the sequence of the hydrolysate.

[0041] Further, in the context of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the term "peptide corresponds to a hydrolysate" is to be understood to encompass a peptide that is either identical to the naturally occurring peptide, in other words, to the peptide that is obtained from the hydrolysis of skeletal muscle protein or is a peptide that has at least about 80% sequence identity with the peptide hydrolysate of skeletal muscle protein, and that maintains the functionality in participating in Milliard process reaction, once heated in the presence of at least one reducing sugar. In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the peptide that corresponds to a hydrolysate in the context of the present disclosure has at least about 85% sequence similarity with a peptide of a hydrolysate of skeletal muscle protein; at times at least about 90% homology; at times, at least about 98% homology, or even at least about 99% homology with a peptide from the hydrolysate of skeletal muscle protein, the level of homology being determined when the peptide is optimally aligned with the naturally occurring peptide to which it is compared.

[0042] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the peptide that corresponds to a hydrolysate has an amino acid sequence identical (100% identity) to the naturally occurring peptide (from the protein hydrolysate).

[0043] The artificially produced peptide can be obtained by any one of hydrolysis of a non-animal protein, e.g. plant protein, expression in vitro (e.g. expression in cultured animal cells, bacteria, yeast, plant etc.), including recombinant expression, 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 meat exudate as the source of the peptide.

[0044] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the peptide that corresponds to a hydrolysate comprises an amino acid sequence having the at least 80% homology while essentially exhibiting the functionality of providing the Maillard flavoring effect in an alternative meat product, with the difference in the sequence being a result of any one or combination of the following,: (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).

[0045] 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 first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the substitution of at least one amino acid to form the functional homologue is a conservative substitution.

[0046] In the context of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, 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, Gin, Glu); Class IV (His, Arg, Lys); Class V (He, Leu, Vai, Met); and Class VI (Phe, Tyr, Trp). For example, substitution of an Asp for another class III residue such as Asn, Gin, or Glu, is a conservative substitution.

[0047] In the context of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, 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, Gin, Glu); Class IV (His, Arg, Lys); Class V (He, Leu, Vai, Met); and Class VI (Phe, Tyr, Trp). For example, substitution of an Asp for another class III residue such as Asn, Gin, 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.

[0048] The presently disclosed composition, according to any one of the first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, has an effect of forming in alternative meat products (e.g. the protein mass infused with the composition) odor-active compounds of the Maillard reaction. The odor-active compounds formed upon heating the presently disclosed alternative meat product provide organoleptic properties, preferably flavor and aroma, that are sufficiently similar to those of a Maillard reaction in a corresponding true meat product (i.e. the animal obtained meat product the alternative meat is aiming at imitating). The similarity can be determined by at least parameter selected from an acceptable sensory 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.

[0049] In the context of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, 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 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.

[0050] The selection of artificially produced peptides that would be suitable for use in the composition, product and / or process as presently disclosed can be based on numerous analytical techniques suitable for analysis of volatile compounds.

[0051] In some examples according to the first, second and / or third disclosed aspects, the selection can be based on a method selected from the group consisting of Gas Chromatography (GC), Mass Spectroscopy (MS), Proton-transfer-reaction mass spectrometry (PTR-MS), High Performance Liquid Chromatography (HPLC), Electronic Chemical Sensor (ECS), and any combination thereof.

[0052] In some examples according to the first, second and / or third disclosed aspects, the selection of artificially produced peptides that would be suitable for use in the composition, product and / or process as presently disclosed can be based on Gas Chromatography coupled with Mass Spectroscopy (GC-MS) techniques, such as those using headspace solid-phase microextraction (SPME). In some examples, the at least one artificially produced peptide is selected by subjecting a test sample containing an examined artificially produced peptide to Gas Chromatography Mass Spectroscopy (GCMS) under conditions that allow formation and extraction of odorants from the test sample, and selecting the artificially produced peptide as suitable for use in the presently disclosed composition, product and / or method, when the extracted odorants correlate with volatile compounds derived from Maillard reaction in animal derived meat.

[0053] In some examples according to the first, second and / or third disclosed aspects, the volatile analysis includes comparison of the detected odorant profiles to a reference library of known compounds associated with desirable sensory characteristics in meat or meat analogs.

[0054] In some examples according to the first, second and / or third disclosed aspects, the reference library includes the odorants listed in Table 2 of Sohail A et al. [ibid.}.

[0055] In some examples, a correlation / or match between the detected odorant / volatile from a tested at least one artificially produced peptide and a referenced odorant (e.g. from a reference library) is determined to be positive when in the GC-MS there is a match factor above 70% and a signal to noise (SNR) ratio that is above 10.

[0056] In some examples according to the first, second and / or third disclosed aspects, the reference library includes at least a compound selected from the group consisting of methanethiol, Benzenemethanethiol, dimethyl sulfide, dimethyl disulfide, dimethyl trisulfide, methional, bi s(2 -furylmethyl) disulfide, 2-methylthiophene, thiazole, benzothiazole, pyrazine, methylpyrazine, 2, 3 -dimethylpyrazine, 2, 5 -dimethylpyrazine, 2,6-dimethylpyrazine, 2-acetylpyrazine, ethylpyrazine, trimethylpyrazine, 2-ethyl-5- methylpyrazine, 2-ethenyl-5(6)-methylpyrazine, 3-ethyl-2,5-dimethylpyrazine, 2- methyl-5-propenylpyrazine, 2,3-diethyl-5-methylpyrazine, pyridine, 2-acetylpyridine, pyrrole, 2-acetylpyrrole, 2-furfurylpyrrole, indole, furfuryl alcohol, 2,3 -butanedione, 1- hydroxy-2-propanone, 3 -hydroxy -butanone, furfural, 2-methyltetrahydrofuran-3-one, 5- methyl-2-furancarboxaldehyde, 2,5-furandicarboxaldehyde, 4-hydroxy-2,5-dimethyl- 3(2H)-furanone, dihydro-2-methyl-3(2H)-furanone, 2-methylpropanal, 2-m ethylbutanal, 3 -methylbutanal, and 2-methylbutanoic acid. These volatiles are also presented in Table 5A below, forming part of the present description.

[0057] In some examples according to the first, second and / or third disclosed aspects, the GC-MS detection used for selecting the at least one artificially produced peptide suitable for use in accordance with the first, second and / or third disclosed aspects, comprises an ionization energy of 70eV and a flow rate ImL / min. In some examples according to the first, second and / or third disclosed aspects, the volatiles collection time for selecting the at least one artificially produced peptide suitable for use in accordance with the first, second and / or third disclosed aspects, is of 15min at 30°C. The injector and MS transfer line temperature was set at 280°C. The oven temperature was set to an initial value of 50°C (held for 3 min) and increased to a final temperature of 260°C at a rate of 10°C / min (held 3min at the final temperature).

[0058] In some examples, the HS-SPME sampling method used for selecting the at least one artificially produced peptide suitable for use in accordance with the first, second and / or third disclosed aspects, comprises 120um DVP / PDMS smart arrow fiber.

[0059] In some examples according to the first, second and / or third disclosed aspects, the correlation between the extracted odorants and volatile compounds derived from Maillard reaction in animal derived meat, for the purpose of selecting an artificially produced peptide is determined based on at least one parameter of gas chromatography.

[0060] In some examples according to the first, second and / or third disclosed aspects, the correlation between the extracted odorants and volatile compounds derived from Maillard reaction in animal derived meat, for the purpose of selecting an artificially produced peptide is determined based on odor activity value equal or greater than 1.

[0061] In the context of the present disclosure, the term “odor activity value” (“OAV”) refers to the ratio between the extracted odorant’s concentration and a pre-determined detection threshold for an odor-active compound with which it correlates (the odor-active compound being, for example, those volatiles listed in Table 2 of Sohail A et al. [ibid.}.

[0062] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation by the selected parameter, e.g. the “odor activity value” for more than one extracted volatile.

[0063] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation by the selected parameter, e.g. the “odor activity value" for more than one extracted volatile.

[0064] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation with at least one extracted volatile, i.e. the at least one artificially produced peptide produces, upon heating under the conditions causing Maillard reaction, at least one volatile selected from the group consisting of methanethiol, Benzenemethanethiol, dimethyl sulfide, dimethyl disulfide, dimethyl trisulfide, methional, bi s(2 -furylmethyl) disulfide, 2- methylthiophene, thiazole, benzothiazole, pyrazine, methylpyrazine, 2,3- dimethylpyrazine, 2, 5 -dimethylpyrazine, 2,6-dimethylpyrazine, 2-acetylpyrazine, ethylpyrazine, trimethylpyrazine, 2-ethyl-5-methylpyrazine, 2-ethenyl-5(6)- methylpyrazine, 3-ethyl-2,5-dimethylpyrazine, 2-methyl-5 -propenylpyrazine, 2,3- diethyl-5-methylpyrazine, pyridine, 2-acetylpyridine, pyrrole, 2-acetylpyrrole, 2- furfurylpyrrole, indole, furfuryl alcohol, 2,3 -butanedione, 1 -hydroxy -2 -propanone, 3- hydroxy-butanone, furfural, 2-methyltetrahydrofuran-3-one, 5-methyl-2- furancarboxaldehyde, 2,5-furandicarboxaldehyde, 4-hydroxy-2,5-dimethyl-3(2H)- furanone, dihydro-2-methyl-3(2H)-furanone, 2-methylpropanal, 2-m ethylbutanal, 3- methylbutanal, and 2-methylbutanoic acid. These volatiles are also presented in Table 5A below, forming part of the present description.

[0065] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation with more than one extracted volatile, i.e. the at least one artificially produced peptide produces, upon heating condition suitable for resulting in Maillard reaction, more than one volatile selected from the group consisting of methanethiol, Benzenemethanethiol, dimethyl sulfide, dimethyl disulfide, dimethyl trisulfide, methional, bi s(2 -furylmethyl) disulfide, 2-methylthiophene, thiazole, benzothiazole, pyrazine, methylpyrazine, 2,3- dimethylpyrazine, 2, 5 -dimethylpyrazine, 2,6-dimethylpyrazine, 2-acetylpyrazine, ethylpyrazine, trimethylpyrazine, 2-ethyl-5-methylpyrazine, 2-ethenyl-5(6)- methylpyrazine, 3-ethyl-2,5-dimethylpyrazine, 2-m ethyl-5 -propenylpyrazine, 2,3- diethyl-5-methylpyrazine, pyridine, 2-acetylpyridine, pyrrole, 2-acetylpyrrole, 2- furfurylpyrrole, indole, furfuryl alcohol, 2,3 -butanedione, 1 -hydroxy -2 -propanone, 3- hydroxy-butanone, furfural, 2-methyltetrahydrofuran-3-one, 5-methyl-2- furancarboxaldehyde, 2,5-furandicarboxaldehyde, 4-hydroxy-2,5-dimethyl-3(2H)- furanone, dihydro-2-methyl-3(2H)-furanone, 2-methylpropanal, 2-m ethylbutanal, 3- methylbutanal, and 2-methylbutanoic acid.

[0066] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation with at least 3 extracted volatiles methanethiol, Benzenemethanethiol, dimethyl sulfide, dimethyl disulfide, dimethyl trisulfide, methional, bi s(2 -furylmethyl) disulfide, 2- methylthiophene, thiazole, benzothiazole, pyrazine, methylpyrazine, 2,3- dimethylpyrazine, 2, 5 -dimethylpyrazine, 2,6-dimethylpyrazine, 2-acetylpyrazine, ethylpyrazine, trimethylpyrazine, 2-ethyl-5-methylpyrazine, 2-ethenyl-5(6)- methylpyrazine, 3-ethyl-2,5-dimethylpyrazine, 2-methyl-5 -propenylpyrazine, 2,3- diethyl-5-methylpyrazine, pyridine, 2-acetylpyridine, pyrrole, 2-acetylpyrrole, 2- furfurylpyrrole, indole, furfuryl alcohol, 2,3 -butanedione, 1 -hydroxy -2 -propanone, 3- hydroxy-butanone, furfural, 2-methyltetrahydrofuran-3-one, 5-methyl-2- furancarboxaldehyde, 2,5-furandicarboxaldehyde, 4-hydroxy-2,5-dimethyl-3(2H)- furanone, dihydro-2-methyl-3(2H)-furanone, 2-methylpropanal, 2-m ethylbutanal, 3- methylbutanal, and 2-methylbutanoic acid.

[0067] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation with at least 5 extracted volatiles selected from the group consisting of methanethiol, Benzenemethanethiol, dimethyl sulfide, dimethyl disulfide, dimethyl trisulfide, methional, bi s(2 -furylmethyl) disulfide, 2-methylthiophene, thiazole, benzothiazole, pyrazine, methylpyrazine, 2, 3 -dimethylpyrazine, 2, 5 -dimethylpyrazine, 2,6- dimethylpyrazine, 2-acetylpyrazine, ethylpyrazine, trimethylpyrazine, 2-ethyl-5- methylpyrazine, 2-ethenyl-5(6)-methylpyrazine, 3-ethyl-2,5-dimethylpyrazine, 2- methyl-5-propenylpyrazine, 2,3-diethyl-5-methylpyrazine, pyridine, 2-acetylpyridine, pyrrole, 2-acetylpyrrole, 2-furfurylpyrrole, indole, furfuryl alcohol, 2,3 -butanedione, 1- hydroxy-2-propanone, 3 -hydroxy -butanone, furfural, 2-methyltetrahydrofuran-3-one, 5- methyl-2-furancarboxaldehyde, 2,5-furandicarboxaldehyde, 4-hydroxy-2,5-dimethyl- 3(2H)-furanone, dihydro-2-methyl-3(2H)-furanone, 2-methylpropanal, 2-m ethylbutanal, 3 -methylbutanal, and 2-methylbutanoic acid.

[0068] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation with at least 8 extracted volatiles selected from the group consisting of methanethiol, Benzenemethanethiol, dimethyl sulfide, dimethyl disulfide, dimethyl trisulfide, methional, bi s(2 -furylmethyl) disulfide, 2-methylthiophene, thiazole, benzothiazole, pyrazine, methylpyrazine, 2, 3 -dimethylpyrazine, 2, 5 -dimethylpyrazine, 2,6- dimethylpyrazine, 2-acetylpyrazine, ethylpyrazine, trimethylpyrazine, 2-ethyl-5- methylpyrazine, 2-ethenyl-5(6)-methylpyrazine, 3-ethyl-2,5-dimethylpyrazine, 2- methyl-5-propenylpyrazine, 2,3-diethyl-5-methylpyrazine, pyridine, 2-acetylpyridine, pyrrole, 2-acetylpyrrole, 2-furfurylpyrrole, indole, furfuryl alcohol, 2,3 -butanedione, 1- hydroxy-2-propanone, 3 -hydroxy -butanone, furfural, 2-methyltetrahydrofuran-3-one, 5- methyl-2-furancarboxaldehyde, 2,5-furandicarboxaldehyde, 4-hydroxy-2,5-dimethyl- 3(2H)-furanone, dihydro-2-methyl-3(2H)-furanone, 2-methylpropanal, 2-m ethylbutanal, 3 -methylbutanal, and 2-m ethylbutanoic acid.

[0069] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation with at least 10 extracted volatiles methanethiol, Benzenemethanethiol, dimethyl sulfide, dimethyl disulfide, dimethyl trisulfide, methional, bi s(2 -furylmethyl) disulfide, 2- methylthiophene, thiazole, benzothiazole, pyrazine, methylpyrazine, 2,3- dimethylpyrazine, 2, 5 -dimethylpyrazine, 2,6-dimethylpyrazine, 2-acetylpyrazine, ethylpyrazine, trimethylpyrazine, 2-ethyl-5-methylpyrazine, 2-ethenyl-5(6)- methylpyrazine, 3-ethyl-2,5-dimethylpyrazine, 2-m ethyl-5 -propenylpyrazine, 2,3- diethyl-5-methylpyrazine, pyridine, 2-acetylpyridine, pyrrole, 2-acetylpyrrole, 2- furfurylpyrrole, indole, furfuryl alcohol, 2,3 -butanedione, 1 -hydroxy -2 -propanone, 3- hydroxy-butanone, furfural, 2-methyltetrahydrofuran-3-one, 5-methyl-2- furancarboxaldehyde, 2,5-furandicarboxaldehyde, 4-hydroxy-2,5-dimethyl-3(2H)- furanone, dihydro-2-methyl-3(2H)-furanone, 2-methylpropanal, 2-m ethylbutanal, 3- methylbutanal, and 2-methylbutanoic acid.

[0070] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation with at least 12 extracted volatiles methanethiol, Benzenemethanethiol, dimethyl sulfide, dimethyl disulfide, dimethyl trisulfide, methional, bi s(2 -furylmethyl) disulfide, 2- methylthiophene, thiazole, benzothiazole, pyrazine, methylpyrazine, 2,3- dimethylpyrazine, 2, 5 -dimethylpyrazine, 2,6-dimethylpyrazine, 2-acetylpyrazine, ethylpyrazine, trimethylpyrazine, 2-ethyl-5-methylpyrazine, 2-ethenyl-5(6)- methylpyrazine, 3-ethyl-2,5-dimethylpyrazine, 2-m ethyl-5 -propenylpyrazine, 2,3- diethyl-5-methylpyrazine, pyridine, 2-acetylpyridine, pyrrole, 2-acetylpyrrole, 2- furfurylpyrrole, indole, furfuryl alcohol, 2,3 -butanedione, 1 -hydroxy -2 -propanone, 3- hydroxy-butanone, furfural, 2-methyltetrahydrofuran-3-one, 5-methyl-2- furancarboxaldehyde, 2,5-furandicarboxaldehyde, 4-hydroxy-2,5-dimethyl-3(2H)- furanone, dihydro-2-methyl-3(2H)-furanone, 2-methylpropanal, 2 -methylbutanal, 3- methylbutanal, and 2-methylbutanoic acid.

[0071] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation with at least 15 extracted volatiles methanethiol, Benzenemethanethiol, dimethyl sulfide, dimethyl disulfide, dimethyl trisulfide, methional, bi s(2 -furylmethyl) disulfide, 2- methylthiophene, thiazole, benzothiazole, pyrazine, methylpyrazine, 2,3- dimethylpyrazine, 2, 5 -dimethylpyrazine, 2,6-dimethylpyrazine, 2-acetylpyrazine, ethylpyrazine, trimethylpyrazine, 2-ethyl-5-methylpyrazine, 2-ethenyl-5(6)- methylpyrazine, 3-ethyl-2,5-dimethylpyrazine, 2-m ethyl-5 -propenylpyrazine, 2,3- diethyl-5-methylpyrazine, pyridine, 2-acetylpyridine, pyrrole, 2-acetylpyrrole, 2- furfurylpyrrole, indole, furfuryl alcohol, 2,3 -butanedione, 1 -hydroxy -2 -propanone, 3- hydroxy-butanone, furfural, 2-methyltetrahydrofuran-3-one, 5-methyl-2- furancarboxaldehyde, 2,5-furandicarboxaldehyde, 4-hydroxy-2,5-dimethyl-3(2H)- furanone, dihydro-2-methyl-3(2H)-furanone 2-methylpropanal, 2-m ethylbutanal, 3- methylbutanal, and 2-methylbutanoic acid.

[0072] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation between volatiles released upon applying conditions of Maillard reaction with at least one volatile selected from the group consisting of Benzothiazole, pyrazine, methylpyrazine, 2,5- dimethylpyrazine, trimethylpyrazine, 2-ethyl-5-methylpyrazine, 3-ethyl-2,5- dimethylpyrazine, 2-acetylpyridine, pyrrole, 2-acetylpyrrole, 2-furfurylpyrrole, furfuryl alcohol, 2,3-butanedione, 1 -hydroxy -2 -propanone, furfural, 2-methyltetrahydrofuran-3- one, 5-methyl-2-furancarboxaldehyde, 2,5-furandicarboxaldehyde and dihydro-2- methyl-3(2H)-furanone.

[0073] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation between volatiles released upon applying conditions of Maillard reaction with at least one volatile selected from the group consisting of pyrazine, methylpyrazine, 2, 5 -dimethylpyrazine, trimethylpyrazine, 2-furfurylpyrrole, 2,3-butanedione, 1 -hydroxy -2 -propanone, furfural, 2-methyltetrahydrofuran-3-one, 5-methyl-2-furancarboxaldehyde and dihydro-2 -methyl- 3(2H)-furanone.

[0074] In some examples of the presently disclosed first, second and / or third aspect, the at least one artificially produced peptide is selected when there is correlation between volatiles released upon applying conditions of Maillard reaction with at least one volatile selected from the group consisting of 2, 5 -dimethylpyrazine, 2-furfurylpyrrole, 2,3- butanedione, 1 -hydroxy -2 -propanone, 2-methyltetrahydrofuran-3-one and dihydro-2 - methyl-3(2H)-furanone.

[0075] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises two or more of the at least one artificially produced peptide.

[0076] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process the 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.

[0077] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the 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.

[0078] In some examples of the presently described first, second and / or third disclosed aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises at least 5 different peptides or between 5 and 40 of the at least one artificially produced peptide. Accordingly, the composition includes at least 5 different artificially produced peptides each corresponding to a different peptide hydrolyzed from the same or different skeletal muscle proteins.

[0079] In some examples of the presently described first, second and / or third disclosed aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises at least 6 or between 6 and 40, at times at least 7 or between 7 and 40, at times, at least 8 or between 8 and 40, at times, at least 9 or between 9 and 40; at times, at least 10 or between 10 and 40; at times, at least 11 or between 11 and 40; at times, at least 12 or between 12 and 40; at times, at least 13 or between 13 and 40; at times, at least 14 or between 14 and 40; at times, at least 15 or between 15 and 40; at times, at least 16 or between 16 and 40; at times, at least 17 or between 18 and 40; at times, at least 18 or between 18 and 40; at times, at least 19 or between 19 and 40 different peptides of the at least one artificially produced peptide.

[0080] In some examples of the presently described first, second and / or third disclosed aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises at least 10 different peptides of the at least one artificially produced peptide.

[0081] In some examples of the presently described first, second and / or third disclosed aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises between 10 and 40 different peptides of the at least one artificially produced peptide.

[0082] In some examples of the presently described first, second and / or third disclosed aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises at least 15 different peptides of the at least one artificially produced peptide.

[0083] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises between 15 and 40 different peptides of the at least one artificially produced peptide. In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process the composition comprises at least 20 different peptides of the at least one artificially produced peptide.

[0084] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises between 20 and 40 different peptides of the at least one artificially produced peptide.

[0085] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises at least 25 different peptides of the at least one artificially produced peptide.

[0086] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises between 25 and 40 different peptides of the at least one artificially produced peptide.

[0087] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises at least 30 different peptides of the at least one artificially produced peptide.

[0088] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises between 30 and 40 different peptides of the at least one artificially produced peptide.

[0089] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises at least 35 different peptides of the at least one artificially produced peptide.

[0090] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises between 35 and 40 different peptides of the at least one artificially produced peptide.

[0091] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises 39 different peptides of the at least one artificially produced peptide.

[0092] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process the composition can comprise any number falling between 5 and 39 of different peptides of the at least one artificially produced peptide.

[0093] The artificially produced peptide(s) can have any number of amino acids between 5 and 20 amino acids.

[0094] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises between 7 and 18 amino acids.

[0095] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0096] 5 amino acids.

[0097] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0098] 6 amino acids.

[0099] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0100] 7 amino acids.

[0101] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises 8 amino acids.

[0102] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0103] 9 amino acids.

[0104] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0105] 10 amino acids.

[0106] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0107] 11 amino acids.

[0108] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0109] 12 amino acids.

[0110] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0111] 13 amino acids.

[0112] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0113] 14 amino acids.

[0114] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0115] 15 amino acids. In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0116] 16 amino acids.

[0117] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0118] 17 amino acids.

[0119] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of the at least one artificially produced peptide comprises

[0120] 18 amino acids.

[0121] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the Maillard flavoring composition comprises at least one additional artificially produced peptide other than those corresponding to a peptide of a skeletal muscle protein.

[0122] The at least one additional artificially produced peptide can arise from different sources.

[0123] The at least one additional artificially produced peptide can arise from different sources.

[0124] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process 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, RTF1 homolog, Pafl / RNA polymerase II complex component, synemin, SYNPO2, nebulin, troponin I, troponin T, titin, dystrophin, myoglobin, tropomyosin, creatine kinase M-type, glyceraldehyde-3 -phosphatase dehydrogenase, carbonic anhydrase 3, Phosphoglycerate kinase 1, and myogenin and beta-enolase. In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is nebulin.

[0125] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is troponin, preferably, troponin T (fast skeletal muscle).

[0126] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is Cysteine and glycine-rich protein 3.

[0127] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is Heat shock protein P6.

[0128] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is Heterogeneous nuclear ribonucleoprotein U.

[0129] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is Scaffold attachment factor A.

[0130] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is keratin.

[0131] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is type I cytoskeletal 9.

[0132] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is LIM domain binding 3. In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is myomesin-1.

[0133] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is RTF1 homolog.

[0134] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is Pafl / RNA polymerase II complex component.

[0135] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is SYNPO2.

[0136] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is beta-enolase.

[0137] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the skeletal muscle protein comprises or is myoglobin.

[0138] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the at least one additional artificially produced peptide corresponds to a hydrolysate peptide of creatine kinase.

[0139] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the at least one additional artificially produced peptide corresponds to a hydrolysate peptide of glyceraldehyde-3 -phosphatase dehydrogenase.

[0140] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the at least one additional artificially produced peptide corresponds to a hydrolysate peptide of carbonic anhydrase 3.

[0141] In some examples of the presently disclosed first, second and / or third disclosed aspects, namely, the disclosed composition, the disclosed product and the disclosed process, the at least one additional artificially produced peptide corresponds to a hydrolysate peptide of Phosphoglycerate kinase l.In some examples, the composition of first, second and / or third disclosed aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, comprises artificially produced peptides and at least one reducing sugar, wherein said artificially produced peptides corresponds to a hydrolysate of skeletal muscle protein selected from the group consisting of LIM domain binding 3, Nebulin, Troponin T, Carbonic anhydrase 3, Creatine kinase M-type, Glyceraldehyde-3 -phosphate dehydrogenase; and wherein upon heating the composition, after infusion into an edible protein mass, a Maillard reaction occurs within the edible protein mass.

[0142] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises at least one reducing sugar, at least one artificially produced peptide corresponding to a peptide hydrolysate of nebulin, and at least one artificially produced peptide that corresponds to a peptide hydrolysate of troponin.

[0143] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises at least one artificially produced peptide that corresponds to a hydrolysate of nebulin, at least one artificially produced peptide that corresponds to a hydrolysate of troponin, at least one artificially produced peptide that corresponds to a hydrolysate of creatine kinase M-type, and at least one artificially produced peptide that corresponds to a hydrolysate of glyceraldehyde-3 -phosphatase dehydrogenase.

[0144] In some examples, the composition of first, second and / or third disclosed aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, comprises artificially produced peptides and at least one reducing sugar, wherein said artificially produced peptides corresponds to a hydrolysate of skeletal muscle protein comprise at least one artificially produced peptide corresponding to a peptide hydrolysate from LIM domain binding 3, at least one artificially produced peptide corresponding to a peptide hydrolysate from Nebulin, at least one artificially produced peptide corresponding to a peptide hydrolysate from Troponin T, at least one artificially produced peptide corresponding to a peptide hydrolysate from Carbonic anhydrase 3, at least one artificially produced peptide corresponding to a peptide hydrolysate from Creatine kinase M-type, and at least one artificially produced peptide corresponding to a peptide hydrolysate from Glyceraldehyde-3 -phosphate dehydrogenase; and wherein upon heating the composition, after infusion into an edible protein mass, a Maillard reaction occurs within the edible protein mass.

[0145] In some examples of the presently disclosed first, second and / or third aspects, the at least one additional artificially produced peptide corresponds to a hydrolysate peptide of Synaptotagmin binding cytoplasmic RNA interacting protein.

[0146] In some examples of the presently disclosed first, second and / or third aspects, the at least one additional artificially produced peptide is in a salt form.

[0147] In some examples of the presently disclosed first, second and / or third aspects, the counter ion of the at least one additional artificially produced peptide is an edible counter ion.

[0148] In some examples of the presently disclosed first, second and / or third aspects, the counter ion of the at least one additional artificially produced peptide is selected from the group consisting of chloride, citrate, phosphate, tartarate, sulphate, acetate and tri fluoroacetates.

[0149] In some examples of the presently disclosed first, second and / or third aspects, the counter ion of the at least one additional artificially produced peptide is an organic counter ion.

[0150] In some examples of the presently disclosed first, second and / or third aspects, the at least one additional artificially produced peptide is in an acetate form.

[0151] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, 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 1 A-1B and any functional homologue of same.

[0152] Table 1A: Artificially Produced Peptides Corresponding to Peptides From Skeletal Muscle Table IB - Artificially Produced Peptides Corresponding to Peptides From RNA interacting protein

[0153] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO: 1.

[0154] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:2.

[0155] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:3.

[0156] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:4.

[0157] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:5.

[0158] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:6. In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO: 7.

[0159] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:8.

[0160] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:9.

[0161] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:10.

[0162] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:11.

[0163] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO: 12.

[0164] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO: 13.

[0165] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO: 14.

[0166] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:15.

[0167] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:16.

[0168] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:17.

[0169] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:18.

[0170] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:19.

[0171] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:20.

[0172] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:21. In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:22.

[0173] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:23.

[0174] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:24.

[0175] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:25.

[0176] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:26.

[0177] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:27.

[0178] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:28.

[0179] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:29.

[0180] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:30.

[0181] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:31.

[0182] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:32.

[0183] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:33.

[0184] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:34.

[0185] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:35.

[0186] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:36. In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:37.

[0187] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:38.

[0188] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the artificially produced peptide comprises or consists of SEQ ID NO:39.

[0189] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, comprises at least one artificially produced peptide having an amino acid sequence as depicted by any one of SEQ ID NO: 5, 6, 11, 24, 26, 27, 31, 33, 36, and 37.

[0190] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, comprises a plurality of the at least one artificially produced peptide, the plurality of the at least one artificially produced peptide comprise or have sequences as depicted in SEQ ID NO: 36; and / or at least one artificially produced peptide comprising or having a sequence as depicted in SEQ ID NO: 31; and / or at least one artificially produced peptide comprising or having a sequence as depicted in SEQ ID NO: 6; and / or at least one artificially produced peptide comprising or having a sequence as depicted in SEQ ID NO: 11 and / or at least one artificially produced peptide comprising or having a sequence as depicted in SEQ ID NO: 24.

[0191] In some examples of the presently disclosed subject matter, the artificially produced peptide comprises or consists of a sequence having at least 80% identity with the amino acid sequence depicted in any one of SEQ ID NO: 1-39 and is capable of participating in a Maillard reaction after infusion into and heating with an edible protein mass, in the presence of at least one reducing sugar.

[0192] As disclosed above, the presently disclosed composition also comprises at least one reducing sugar.

[0193] In the context of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, 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).

[0194] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the at least one reducing sugar comprises or is a saccharide containing molecule.

[0195] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, 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.

[0196] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the at least one reducing sugar comprises or is a disaccharide. A nonlimiting list of disaccharides includes maltose, cellobiose and lactose.

[0197] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, 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 first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition comprises two or more reducing sugars.

[0198] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the at least one reducing sugar comprises at least ribose.

[0199] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the at least one reducing sugar comprises ribose and dextrose.

[0200] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the at least one reducing sugar comprises, the presently disclosed composition also comprises at least one amino acid monomer.

[0201] In the context of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, 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.

[0202] 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 (He, I), Leucine (Leu, L), Lysine (Lys, K), Methionine (Met, M), Asparagine (Asn, N), Glutamine (Gin, 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.

[0203] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the amino acid monomer is selected from glutathione, taurine, ornithine, carnosine, cystine, citrulline, P-alanine.

[0204] Without being bound thereto, it has been now found that adding free amino acid monomers, such as those listed above, can boost the organoleptic properties, and specifically the meaty flavor and aroma, preferably when combined with said at least one amino acid. 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.

[0205] Table 2: Free Amino Acid Relative Amounts

[0206] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the relative amount of each free amino acids in the composition, is between 0.01 and 25% out of total amount of the free amino acids.

[0207] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of Ala, Gin, and Gly and Leu are each present in an amount of between 5% and 25% out of total amount of the free amino acids.

[0208] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of Ala, Gin and Gly are each present in an amount of between 10% and 25% out of total amount of the free amino acids.

[0209] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least one of Ala and Gin are each present in an amount of between 15% and 25% out of total amount of the free amino acids.

[0210] The presently disclosed composition can be provided in any physical form, including dry, semi-dry / semi-liquid, and liquid form.

[0211] In some examples of the presently disclosed subject matter, the presently disclosed composition is in dry form, this includes, without being limited thereto, dehydrated or lyophilized.

[0212] In some examples of the presently disclosed subject matter, the presently disclosed composition is in semi-dried form, e.g. paste like form.

[0213] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the composition is animal-free. In the context of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, when referring to an "animal free" composition or product it is to be understood that at least the at least one peptide in the composition is not derived or obtained from an animal source, e.g. from an exudate of animal part. Yet, in the context of “animal free” it is to be understood that the at least one artificially produced peptide can be derived from cultured animal cells.

[0214] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the Maillard flavoring composition is absence of any component or ingredient that was obtained or derived from animal source.

[0215] The presently disclosed composition is preferably for use in creating a Maillard reaction in the meat product into which it is introduced, and thereby providing a flavor or aroma to alternative meat products once the alternative meat product holding the composition is heated, e.g. cooked, fried, backed, roasted, grilled, pan-seared, broiled, barbecued. It has been found that the presently disclosed composition is effective to provide the desired flavor (taste and aroma), once heated with the protein mass of the alternative meat product, 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.

[0216] For example, a composition according to the presently disclosed first, second and / or third aspects, is designed for an alternative Sirloin meat product would provide the animal free / plant based alternative Sirloin meat product with taste and aroma similar to a true Sirloin cut.

[0217] In line with the above, the presently disclosed subject matter also provides, in accordance with a second of its aspects, an alternative meat product an alternative meat / edible protein mass infused with the presently disclosed composition, such that upon heating, a Maillard reaction takes place in the alternative meat product infused with the disclosed composition.

[0218] Specifically, the presently disclosed subject matter also provides an alternative meat product comprising an alternative meat / edible protein mass infused or holding a composition comprising at least one artificially produced peptide and at least one reducing sugar, wherein the at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein; and wherein upon heating the composition, after infusion into an edible protein mass, a Maillard reaction occurs within the edible protein mass.

[0219] For simplicity, all definitions and terms used with respect to the presently disclosed composition also apply to the presently disclosed alternative meat product.

[0220] The alternative meat product disclosed herein can be of any type and form.

[0221] In some examples of the presently disclosed subject matter, the alternative meat product is an alternative whole muscle cut.

[0222] In some examples of the presently disclosed subject matter, the alternative meat product is an alternative minced meat.

[0223] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the edible protein mass comprises protein(s) that are 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).

[0224] In the context of the first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, 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 “intermediate” form of texturized vegetable protein, in which the moisture level in the TVP and / or the degree of expansion of the TVP is intermediate between those typically found in dry (expanded) form and HME(C) form.

[0225] The protein(s) of the alternative meat / edible 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 first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, 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.

[0226] The protein of the protein(s) mass may include a single type of protein or a blend of proteins.

[0227] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, at least some of the proteins of the protein mass contain a recombinant protein, derived from e.g. plants, algae, fungi, and / or microorganisms.

[0228] 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 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).

[0229] As noted above, the protein mass is infused (e.g. marinated) with the presently disclosed composition. The infusion can be to an extent that the presently disclosed composition penetrates into the protein mass, or at least into portions of the protein mass.

[0230] As used herein, the term "infused" denotes the process or the result of the process by which the disclosed composition permeates and becomes incorporated into the protein mass of the meat alternative product. The infusion involves the introduction of the presently disclosed 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 (including immersing the edible protein mass in the composition and optionally coating the edible protein mass with the composition and / or injecting the composition into the edible protein mass) or by any other means of or any other suitable technique that facilitates the uniform distribution of the flavoring composition within and over the protein mass.

[0231] In some examples of the presently disclosed first, second and / or third aspects, namely, the disclosed composition per se, as part of the disclosed product or as part of the disclosed process, the protein mass of the alternative meat product is constructed as a muscle scaffold / protein matrix.

[0232] 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 alternative meat / edible protein mass with a composition comprising at least one artificially produced peptide and at least one reducing sugar, wherein the at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein; and wherein upon heating the composition, after infusion into an edible protein mass, a Maillard reaction occurs within the edible protein mass. The infusion, as described above, is the process by which the presently disclosed composition permeates and becomes incorporated into the protein mass of the meat alternative.

[0233] 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.

[0234] 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.

[0235] As used herein in the specification and in the claim, the form “and / or ” should be understood to mean “either or both” of the elements so conjoined, i.e., elements that are conjunctively present in some cases and disjunctively present in other cases. Multiple elements listed with “and / or” should be construed in the same fashion, i.e., “one or more” of 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.

[0236] 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.

[0237] 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.

[0238] 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.

[0239] LIST OF PARAGRAPHS

[0240] The following statements / paragraphs disclose features of the present disclosure. It is to be appreciated that any combination of these two or more of these paragraphs, or parts of paragraphs, constitute part of the invention and that there should be no limitation to the number of paragraphs that can be combined, as part of the presently disclosed subject matter:

[0241] 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; and wherein upon heating the composition, after infusion into an edible protein mass, a Maillard reaction occurs within the edible protein mass.

[0242] 2. The composition of pharagraph 1, comprising two or more of said at least one artificially produced peptide.

[0243] 3. The composition of any one of the above paragraphs, 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.

[0244] 4. The composition of any one of the above paragraphs, 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.

[0245] 5. The composition of of any one of the above paragraphs, comprising at least 5 of said at least one artificially produced peptide.

[0246] 6. The composition of of any one of the above paragraphs, wherein said at least one artificially produced peptide is selected by subjecting a test sample comprising at least one artificially produced peptide to Gas Chromatography Mass Spectroscopy (GC-MS) under conditions that allow formation and extraction of odorants from the test sample; and selecting the at least one artificially produced peptide as suitable for use in said composition, when said odorants correlate with volatile compounds derived from Maillard reaction in animal derived meat.

[0247] 7. The composition of pharagraph 6, wherein correlation is determined based on at least one parameter of gas chromatography and / or on odor activity value equal or greater than 1.

[0248] 8. The composition of paragraph 6 or 7, wherein said at least one artificially produced peptide is selected, when the peptide correlates with at least 5 volatile compounds derived from Maillard reaction in animal derived meat.

[0249] 9. The composition of any one of the above paragraphs, 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. 10. The composition of any one of the above paragraphs, wherein said at least one artificially produced peptide comprises between 5 and 20 amino acids.

[0250] 11. The composition of any one of the above paragraphs, wherein said at least one artificially produced peptide comprises between 7 and 18 amino acids.

[0251] 12. The composition of of any one of the above paragraphs, wherein said 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, Pafl / RNA polymerase II complex component, synemin, SYNPO2, nebulin, troponin I, troponin T, titin, dystrophin, tropomyosin, myogenin, creatine kinase M-type, glyceraldehyde-3 -phosphatase dehydrogenase, carbonic anhydrase 3, Phosphoglycerate kinase 1, beta-enolase and myoglobin.

[0252] 13. The composition of any one of the above paragraphs, wherein said skeletal muscle protein is nebulin.

[0253] 14. The composition of any one of the above paragraphs, wherein said skeletal muscle protein is troponin.

[0254] 15. The composition of any one of the above paragraphs, wherein said skeletal muscle protein is creatine kinase M-type.

[0255] 16. The composition of any one of the above paragraphs, wherein said skeletal muscle protein is glyceraldehyde-3 -phosphatase dehydrogenase.

[0256] 17. The composition of any one of the above paragraphs, comprising at least one artificially produced peptide that corresponds to a hydrolysate of nebulin, at least one artificially produced peptide that corresponds to a hydrolysate of troponin, at least one artificially produced peptide that corresponds to a hydrolysate of creatine kinase M-type, and at least one artificially produced peptide that corresponds to a hydrolysate of glyceraldehyde-3 -phosphatase dehydrogenase.

[0257] 18. The composition of any one of the above paragraphs, comprising at least one additional artificially produced peptide that corresponds to a hydrolysate of a protein selected from the group consisting ofSynaptotagmin binding cytoplasmic RNA interacting protein. 19. The composition of any one of the above paragraphs, wherein said at least one artificially produced peptide is in a salt form.

[0258] 20. The composition of any one of the above paragraphs, comprising at least one artificially produced peptide comprises or consists of an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO:39 and / or an amino acid sequence having at least 80% identity with an amino acid sequence as depicted in any one of SEQ ID NO:1 to SEQ ID NO:39, and capable of participating in a Maillard reaction once infused into and heated with an edible protein mass, in the presence of at least one reducing sugar.

[0259] 21. The composition of any one of the above paragraphs, comprising between about 5 and 39 of said at least one artificially produced peptide.

[0260] 22. The composition of any one of the above paragraphs, 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.

[0261] 23. The composition of any one of the above paragraphs, wherein said at least one reducing sugar comprises at least ribose.

[0262] 24. The composition of any one of the above paragraphs, comprising two or more reducing sugars.

[0263] 25. The composition of any one of the above paragraphs, wherein said at least one reducing sugar comprises ribose and dextrose.

[0264] 26. The composition of any one of the above paragraphs, comprising at least one amino acid monomer.

[0265] 27. The composition of paragraph 26, wherein said at least one amino acid monomer is selected from the group consisting of glutathione, taurine, ornithine, carnosine, cystine, citrulline, P-alanine.

[0266] 28. The composition of any one of the above paragraphs, in dry form.

[0267] 29. The composition of any one of the above paragraphs, being animal-free.

[0268] 30. An alternative meat product comprising an edible protein mass infused with a composition comprising at least one artificially produced peptide and at least one reducing sugar, wherein the at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein; and wherein upon heating the composition, after infusion into an edible protein mass, a Maillard reaction occurs within the edible protein mass.

[0269] 31. An alternative meat product of paragraph 30, comprising two or more of said at least one artificially produced peptide.

[0270] 32. The alternative meat product of paragraph 31, 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.

[0271] 33. The alternative meat product of paragraph 31 or 32, 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.

[0272] 34. The alternative meat product any one of the above paragraphs, comprising at least 5 of said at least one artificially produced peptide.

[0273] 35. The alternative meat product of any one of the above paragraphs, wherein said at least one artificially produced peptide is selected by subjecting a test sample comprising at least one artificially produced peptide to Gas Chromatography Mass Spectroscopy (GC-MS) under conditions that allow formation and extraction of odorants from the test sample; and selecting the at least one artificially produced peptide as suitable for use in said composition, when said odorants correlate with volatile compounds derived from Maillard reaction in animal derived meat.

[0274] 36. The alternative meat product of any one of the above paragraphs, wherein correlation is determined based on at least one parameter of gas chromatography and / or on odor activity value equal or greater than 1.

[0275] 37. The alternative meat product any one of the above paragraphs, wherein said at least one artificially produced peptide is selected when it correlates with at least 5 volatile compounds derived from Maillard reaction in animal derived meat.

[0276] 38. The alternative meat product any one of the above paragraphs, 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. 39. The alternative meat product any one of the above paragraphs, wherein said at least one artificially produced peptide comprises between 5 and 20 amino acids.

[0277] 40. The alternative meat product any one of the above paragraphs, wherein said at least one artificially produced peptide comprises between 7 and 18 amino acids.

[0278] 41. The alternative meat product any one of the above paragraphs, wherein said 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, Pafl / RNA polymerase II complex component, synemin, SYNPO2, nebulin, troponin I, troponin T, titin, dystrophin, tropomyosin, myogenin, creatine kinase M-type, glyceraldehyde-3 -phosphatase dehydrogenase, carbonic anhydrase 3, Phosphoglycerate kinase 1, beta-enolase and myoglobin.

[0279] 42. The alternative meat product any one of the above paragraphs, wherein said skeletal muscle protein is nebulin.

[0280] 43. The alternative meat product any one of the above paragraphs, wherein said skeletal muscle protein is troponin.

[0281] 44. The alternative meat product any one of the above paragraphs, wherein said skeletal muscle protein is creatine kinase M-type.

[0282] 45. The alternative meat product any one of the above paragraphs, wherein said skeletal muscle protein is glyceraldehyde-3 -phosphatase dehydrogenase.

[0283] 46. The alternative meat product any one of the above paragraphs, comprising at least one artificially produced peptide that corresponds to a hydrolysate of nebulin, at least one artificially produced peptide that corresponds to a hydrolysate of troponin, at least one artificially produced peptide that corresponds to a hydrolysate of creatine kinase M-type, and at least one artificially produced peptide that corresponds to a hydrolysate of glyceraldehyde-3 -phosphatase dehydrogenase.

[0284] 47. The alternative meat product any one of the above paragraphs, comprising at least one additional artificially produced peptide that corresponds to a hydrolysate of a protein selected from the group consisting of Synaptotagmin binding cytoplasmic RNA interacting protein. 48. The alternative meat product any one of the above paragraphs, wherein said at least one artificially produced peptide is in a salt form.

[0285] 49. The alternative meat product any one of the above paragraphs, comprising at least one artificially produced peptide comprises or consists of an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO: 39 and / or an amino acid sequence having at least 80% identity with an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO:39, and capable of participating in a Maillard reaction once infused into and heated with an edible protein mass, in the presence of at least one reducing sugar.

[0286] 50. The alternative meat product any one of the above paragraphs, comprising between about 5 and 39 of said at least one artificially produced peptide.

[0287] 51. The alternative meat product any one of the above paragraphs, 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.

[0288] 52. The alternative meat product any one of the above paragraphs, wherein said at least one reducing sugar comprises at least ribose.

[0289] 53. The alternative meat product any one of the above paragraphs, comprising two or more reducing sugars.

[0290] 54. The alternative meat product any one of the above paragraphs, wherein said at least one reducing sugar comprises ribose and dextrose.

[0291] 55. The alternative meat product any one of the above paragraphs, comprising at least one amino acid monomer.

[0292] 56. The alternative meat product any one of the above paragraphs, wherein said at least one amino acid monomer is selected from the group consisting of glutathione, taurine, ornithine, carnosine, cystine, citrulline, P-alanine.

[0293] 57. The alternative meat product any one of the above paragraphs, wherein said composition is infused into said edible protein mass.

[0294] 58. The alternative meat product any one of the above paragraphs, wherein said edible protein mass comprises a plant protein. 59. The alternative meat product any one of the above paragraphs, wherein said plant protein comprises texturized vegetable protein (TVP).

[0295] 60. The alternative meat product any one of the above paragraphs, being animal free.

[0296] 61. The alternative meat product any one of the above paragraphs, wherein said edible protein mass is in a form of a muscle scaffold.

[0297] 62. A process of producing an alternative meat product comprising infusing an edible protein mass with a composition suitable for forming a Maillard reaction following heating of said alternative meat product, said composition comprises at least one artificially produced peptide and at least one reducing sugar, wherein the at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein .

[0298] 63. The process of paragraph 62, wherein said infusing of the composition is by marination.

[0299] 64. The process any one of the above paragraphs, wherein said composition comprises two or more of said at least one artificially produced peptide.

[0300] 65. The process any one of the above paragraphs, 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.

[0301] 66. The process any one of the above paragraphs, wherein said composition comprises at least 5 of said at least one artificially produced peptide.

[0302] 67. The process any one of the above paragraphs, wherein said at least one artificially produced peptide in said composition is selected by subjecting a test sample comprising at least one artificially produced peptide to Gas Chromatography Mass Spectroscopy (GC-MS) under conditions that allow formation and extraction of odorants from the test sample; and selecting the at least one artificially produced peptide as suitable for use in said composition, when said odorants correlate with volatile compounds derived from Maillard reaction in animal derived meat. 68. The process of any one of the above paragraphs, wherein correlation is determined based on at least one parameter of gas chromatography and / or on odor activity value equal or greater than 1.

[0303] 69. The process any one of the above paragraphs, wherein said at least one artificially produced peptide is selected when it correlates with at least 5 volatile compounds derived from Maillard reaction in animal derived meat.

[0304] 70. The process any one of the above paragraphs, 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.

[0305] 71. The process any one of the above paragraphs, wherein said at least one artificially produced peptide comprises between 5 and 20 amino acids.

[0306] 72. The process any one of the above paragraphs, wherein said at least one artificially produced peptide comprises between 7 and 18 amino acids.

[0307] 73. The process any one of the above paragraphs, wherein said 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, Pafl / RNA polymerase II complex component, synemin, SYNPO2, nebulin, troponin I, troponin T, titin, dystrophin, tropomyosin, myogenin, creatine kinase M-type, glyceraldehyde-3 -phosphatase dehydrogenase, carbonic anhydrase 3, Phosphoglycerate kinase 1, beta-enolase and myoglobin.

[0308] 74. The process any one of the above paragraphs, wherein said skeletal muscle protein is nebulin.

[0309] 75. The process any one of the above paragraphs, wherein said skeletal muscle protein is troponin.

[0310] 76. The process any one of the above paragraphs, wherein said skeletal muscle protein is creatine kinase M-type.

[0311] 77. The process any one of the above paragraphs, wherein said skeletal muscle protein is glyceraldehyde-3 -phosphatase dehydrogenase. 78. The process any one of the above paragraphs, wherein said composition comprises at least one of said at least one artificially produced peptide that corresponds to a hydrolysate of nebulin, at least one of said at least one artificially produced peptide that corresponds to a hydrolysate of troponin, at least one of said at least one artificially produced peptide that corresponds to a hydrolysate of creatine kinase M-type, and at least one of said at least one artificially produced peptide that corresponds to a hydrolysate of glyceraldehyde-3- phosphatase dehydrogenase.

[0312] 79. The process any one of the above paragraphs, wherein said composition comprises at least one additional artificially produced peptide that corresponds to a hydrolysate of a protein selected from the group consisting of Synaptotagmin binding cytoplasmic RNA interacting protein.

[0313] 80. The process any one of the above paragraphs, wherein said at least one artificially produced peptide is in a salt form.

[0314] 81. The process any one of the above paragraphs, wherein said composition comprises at least one artificially produced peptide comprises or consists of an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO: 39 and / or an amino acid sequence having at least 80% identity with an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO:39, and capable of participating in a Maillard reaction once infused into and heated with an edible protein mass, in the presence of at least one reducing sugar.

[0315] 82. The process any one of the above paragraphs, wherein said composition comprises between about 5 and 39 of said at least one artificially produced peptide.

[0316] 83. The process any one of the above paragraphs, wherein said at least one reducing sugar of said composition is selected from the group consisting of glucose, glucose-6 phosphate, galactose, fructose, ribose, maltose, glyceraldehyde, xylose, cellobiose, lactose.

[0317] 84. The process any one of the above paragraphs, wherein said at least one reducing sugar of said composition comprises at least ribose.

[0318] 85. The process any one of the above paragraphs, wherein said composition comprises two or more reducing sugars.

[0319] 86. The process any one of the above paragraphs, wherein said at least one reducing sugar of said composition comprises ribose and dextrose. 87. The process any one of the above paragraphs, wherein said composition comprises at least one amino acid monomer.

[0320] 88. The process any one of the above paragraphs, wherein said at least one amino acid monomer is selected from the group consisting of glutathione, taurine, ornithine, carnosine, cystine, citrulline, P-alanine.

[0321] 89. The process any one of the above paragraphs, wherein said edible protein mass comprises a plant protein.

[0322] 90. The process any one of the above paragraphs, wherein said plant protein comprises texturized vegetable protein (TVP).

[0323] 91. The process any one of the above paragraphs, wherein said edible protein mass and said composition are animal free.

[0324] 92. The process any one of the above paragraphs, wherein said edible protein mass is in a form of a muscle scaffold.

[0325] DESCRIPTION OF NON-LIMITING EXAMPLES

[0326] In the following non-limiting examples, the following equipment was used:

[0327] Ultrafiltration - was performed using Amicon® Ultra-15 Centrifugal-Filter Unit devices (Ultracel® regenerated cellulose membrane with either a lOkDa or 3kDa cutoff).

[0328] Gel filtration - was performed using Sephadex G-25 resin (Cytiva).

[0329] Solid phase extraction - was performed using Oasis HLB reversed-phase sorbent (Waters) and Oasis MCX mixed-mode cationic sorbent (Waters).

[0330] 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).

[0331] 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 pure™ protein purification system equipped with Superdex 30 Increase column, suitable for the purification and analysis of peptides in the range 100-7000 Da to.

[0332] Measurement of peptides concentrations - was performed using NanoDrop™ OnecMicrovolume UV-Vis spectrophotometer.

[0333] 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 pm 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 pm).

[0334] Example 1: Peptides extraction and characterization

[0335] 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.

[0336] 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.

[0337] At a first stage, aqueous components of raw meat (referred to herein as the meat juice “MJ”) were extracted and added to a TVP -based composition (the protein mass) and the combined MJ-protein mass was then subjected to cooking at 175°C for 3 min, and then tested for flavor and aroma (F&A) in both sensory (tasting and sniffing panels) and analytical (GC-MS) tests. The GC-MS examined all recorded volatiles after cooking and compared them to volatiles reported as “meaty” in existing literature as listed in Table 2 of Sohail et al., ibid. All the aqueous components that correlated with the reported volatiles (i.e. appeared both in the GC-MS and in the aforesaid literature) with a threshold having a match factor of 70% and signal to noise ratio (SNR) that is above 10, were listed as significant volatiles, and these are shown in Table 5 A below. In a parallel test, the MJ was filtered through Amicon 0.15 micron filter, to remove high MW and insoluble substances. It was shown that also the filtered MJ maintained the F&A characteristic the beef meat of origin.

[0338] To identify the peptides in the MJ, the following experiments and analyses were performed:

[0339] Peptidomics: LC-MS analysis

[0340] Two MJ were obtained and analyzed by LC-MS, one from sirloin and another 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 lOkDa from other (larger than lOkDa) components in the MJ.

[0341] 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).

[0342] 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.

[0343] 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.

[0344] The molecular weight distributions of the MJ peptides from the sirloin cut and from the meat chuck are provided in Figures 1A and IB, respectively.

[0345] 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.

[0346] Sample preparation and size-exclusion fast protein liquid chromatography (FPLC)

[0347] 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.

[0348] Specifically, MJ was centrifuged extensively by ultracentrifugation (400,000 g) to remove solids and aggregates. The supernatant was filtered using a 0.45pm and then centrifuged using Amicon® ultrafiltration devices with a 3 kDa molecular cutoff, yielding the final clear liquid phase in the flow-through.

[0349] 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 ImL PBS to be used as a single second injection (see in this connection Figure 2B).

[0350] 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).

[0351] 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 7 different peaks, identified as peaks A, B, C, D, E, F, G, as further discusses below.

[0352] 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. Sensory test of FPLC-isolated fractions

[0353] The seven 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.

[0354] 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. In the absence of externally added ribose, Maillard reaction also occurred, yet to a much lower extent, and this may be explained by the inherent presence of reducing sugars from the meat juice.

[0355] 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.

[0356] The fractions concentrations were measured using the Nanodrop and the A205 method, in which an extinction coefficient of 31 mL mg-lcm-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 al 205 nm" Analytical Biochemistry. 59:277-282 (1974)].

[0357] 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. Properties o f the peptides in fractions B and C

[0358] As noted above, 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.

[0359] 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.

[0360] 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 IB, 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.

[0361] 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.

[0362] Table 3 provides a list of 39 peptides from fraction C, that contributed to Maillard reaction and meat process flavor, as determined using the aforesaid Peptidomics of FPLC fractions. It is noted that this fraction was selected for convenience (a fewer number of peptides to isolate and identify) and a similar analysis can be made with other fractions. Table 3 - Selected peptides as meat process flavors

[0363] 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

[0364] Preparation of peptides samples for GCMS runs:

[0365] Out of the 39 peptides listed in Table 3, 11 peptides were chemically synthesized (Biosynth Company), with each peptide produced in two variants, acetate-terminated and chloride-terminate (thus resulting in 22 peptides). The synthetized peptides were received in lyophilized form (each 25MG), for subsequent analysis. The peptides were numbered for convenience as shown in Table 4.

[0366] Table 4 - Selected peptides The total 22 peptides (11 peptides in two different salt forms) were dissolved in

[0367] 0.25mL 50mM Sodium Phosphate buffer (pH 7.4) directly in the GC vials.

[0368] Peptides numbered 2, 6, 10 did not fully dissolve, which required the addition of a total 0.5mL buffer, which still resulted as turbid. A separate stock solution of mixed Dextrose and Ribose, at 0.2M each, was prepared using the same Sodium Phosphate buffer.

[0369] To each GC vial, 24-56uL Dex+Ribose (“reducing sugar”), lOOuL of peptide and the corresponding volume of sodium phosphate were added to reach a 1 : 1 molar ratio between the reducing sugars and the peptide. The total reaction volume for each peptide was 200uL.

[0370] The vials were heated to a set temperature of 160°C for a period of 10 min.

[0371] As negative control, Dextrose +Ribose solution without a peptide, was used.

[0372] Gas Chromatography Mass Spectroscopy (GC-MS)

[0373] Each of the 22 tested peptides was tested in GC-MS, after heating in solution, with Dextrose +Ribose (0.2M for each), required for Maillard reaction. As control, a sample containing the primary sugars only, was used.

[0374] Specifically, the following sample preparation protocol was used:

[0375] Each of the peptides was dissolved in 0.25mL 50mM Sodium Phosphate buffer (pH 7.4) directly in the vials.

[0376] Peptides 2, 6, 10 did not fully dissolve and therefore, buffer was added to a total 0.5mL buffer, although the solution was still turbid.

[0377] A separate stock solution of mixed Dextrose and Ribose, at 0.2M each, was prepared using the same buffer above.

[0378] To each GC vial added the 24-56uL Dex+Ribose, lOOuL of peptide and the corresponding volume of sodium phosphate to reach a 1 : 1 molar ratio between the reducing sugars and the peptide. The total reaction volume for each peptide was 200uL.

[0379] The vials were heated using the GC heater set to 160C and 10 min.

[0380] The negative controls were Dex+Ribose and sodium phosphate.

[0381] GC-MS detection was performed using an ionization energy of 70eV and a flow rate ImL / min. For the HS-SPME sampling method (120um DVP / PDMS smart arrow fiber), a luL injection volume was used. Volatiles collection time of 15min at 30°C was used. The injector and MS transfer line temperature was set at 280°C. The oven temperature was set to an initial value of 50°C (held for 3 min) and increased to a final temperature of 260°C at a rate of 10°C / min (held 3min at the final temperature). Data deconvolution was performed using a matching factor of 50% and a signal to noise ratio of 2.

[0382] Identification of "meaty" volatiles: Table 5 A summarizes volatile compounds known to be produced in meaty food

[0383] (according to Table 2 of Sohail et al., ibidf and for which a corresponding volatile compound was produced by the tested peptides. Each volatile known to be produced in meaty food, was given an arbitrary number #.

[0384] Table 5A: list of volatile compounds and their animal origin

[0385]

[0386] The presence of the above volatiles was tested in two animal derived samples, including raw (uncooked) sirloin (negative control), cooked sirloin, and cooked meat juice (from sirloin). The cooked samples were subjected to 175°C, the meat juice to 3 minutes cooking while the other samples, in mashed form, to 10 minutes cooking, to ensure the formation of Maillard process flavors.

[0387] Table 5B shows that the cooked samples (be it the sirloin meat or the cooked meat juice) provided some of the volatile’s characteristic of Maillard reaction, as detailed in Table 5 A, while the uncooked sample exhibited no volatiles formation. Table 5B- presence of volatiles in animal derived samples

[0388] It has been found that some of the tested peptides provided a single volatile compound out of Table 5A, and some even up to 20. Table 5C summarizes the number of volatiles extracted from each peptide (according to the peptide numbering in Table 4) and the numbers of the volatiles, according to Table 5A. Further shown in Table 5C are the volatiles extracted when all the chloride salt peptides were mixed (All chloride) or all the acetate salt peptides were mixed (All acetate).

[0389] Table 5C- Extracted volatile correlation to meaty volatiles Peptide

[0390] The data presented in Table 5C shows some interesting observations. One unique observation is that peptides being in their salt form (in this specific example, provided as an acetate salt). When the peptide is in its salt form, the number of extracted volatiles characteristic of Maillard reaction was greater as compared to the volatiles obtained when in non-salt form. This is exhibited with all the sequences, where peptides 1 to 11 (in nonsalt form) provided half the number of volatiles as comparted to the same sequence in the acetate form.

[0391] Alternative meat product Figure 4 provides GC-MS of a Ribeye beef loin slice before and after cooking at

[0392] 175°C till reaching 65°C in the middle. The difference in volatile profile before and after cooking is evident.

[0393] To show the effect of the presently disclosed composition, an alternative meat product will be produced with the presently disclosed composition and the GC-MS of the uncooked or cooked alternative meat product will be provided.

[0394] As control, the composition of hydrolysates without reducing sugar will also be used.

[0395] It is expected that the alternative meat product before cooking on absent of the reducing sugar will provide a same volatile profile as that of the uncooked Ribeye beef loin slice of Figure 4, while the cooked (under the same condition) alternative meat product including the hydrolysates and reducing sugar, as defined herein, will provide a GC-MS volatile profile resembling that of the cooked Ribeye beef loin slice.

Claims

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; and wherein upon heating the composition, after infusion into an edible protein mass, a Maillard reaction occurs within the edible protein mass.

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

3. The Maillard flavoring 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 3, 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 said at least one artificially produced peptide is selected by- subjecting a test sample comprising at least one artificially produced peptide to Gas Chromatography Mass Spectroscopy (GC-MS) under conditions that allow formation and extraction of odorants from the test sample; and- selecting the at least one artificially produced peptide as suitable for use in said composition, when said odorants correlate with volatile compounds derived from Maillard reaction in animal derived meat.

7. The composition of claim 6, wherein correlation is determined based on at least one parameter of gas chromatography and / or on odor activity value equal or greater than 1.

8. The composition of claim 6 or 7, wherein said at least one artificially produced peptide is selected, when the peptide correlates with at least 5 volatile compounds derived from Maillard reaction in animal derived meat.

9. The composition of any one of claims 1 to 8, 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.

10. The composition of any one of claims 1 to 9, wherein said at least one artificially produced peptide comprises between 5 and 20 amino acids.

11. The composition of any one of claims 1 to 10, wherein said at least one artificially produced peptide comprises between 7 and 18 amino acids.

12. The composition of any one of claims 1 to 11, wherein said 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, Pafl / RNA polymerase II complex component, synemin, SYNPO2, nebulin, troponin I, troponin T, titin, dystrophin, tropomyosin, myogenin, creatine kinase M-type, glyceraldehyde-3 -phosphatase dehydrogenase, carbonic anhydrase 3, Phosphoglycerate kinase 1, beta-enolase and myoglobin.

13. The composition of any one of claims 1 to 12, wherein said skeletal muscle protein is nebulin.

14. The composition of any one of claims 1 to 12, wherein said skeletal muscle protein is troponin.

15. The composition of any one of claims 1 to 12, wherein said skeletal muscle protein is creatine kinase M-type.

16. The composition of any one of claims 1 to 12, wherein said skeletal muscle protein is glyceraldehyde-3 -phosphatase dehydrogenase.

17. The composition of any one of claims 1 to 16, comprising at least one artificially produced peptide that corresponds to a hydrolysate of nebulin, at least one artificially produced peptide that corresponds to a hydrolysate of troponin, at least one artificially produced peptide that corresponds to a hydrolysate of creatine kinase M-type, and at leastone artificially produced peptide that corresponds to a hydrolysate of glyceraldehyde-3- phosphatase dehydrogenase.

18. The composition of any one of claims 1 to 17, comprising at least one additional artificially produced peptide that corresponds to a hydrolysate of a protein selected from the group consisting ofSynaptotagmin binding cytoplasmic RNA interacting protein.

19. The composition of any one of claims 1 to 18, wherein said at least one artificially produced peptide is in a salt form.

20. The composition of any one of claims 1 to 19, comprising at least one artificially produced peptide comprises or consists of an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO:39 and / or an amino acid sequence having at least 80% identity with an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO: 39, and capable of participating in a Maillard reaction once infused into and heated with an edible protein mass, in the presence of at least one reducing sugar.

21. The composition of any one of claims 1 to 20, comprising between about 5 and 39 of said at least one artificially produced peptide.

22. The composition of any one of claims 1 to 21, 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.

23. The composition of any one of claims 1 to 22, wherein said at least one reducing sugar comprises at least ribose.

24. The composition of any one of claims 1 to 23, comprising two or more reducing sugars.

25. The composition of any one of claims 1 to 24, wherein said at least one reducing sugar comprises ribose and dextrose.

26. The composition of any one of claims 1 to 25, comprising at least one amino acid monomer.

27. The composition of claim 26, wherein said at least one amino acid monomer is selected from the group consisting of glutathione, taurine, ornithine, carnosine, cystine, citrulline, P-alanine.

28. The composition of any one of claims 1 to 27, in dry form.

29. The composition of any one of claims 1 to 28, being animal-free.

30. An alternative meat product comprising an edible protein mass infused with a composition comprising at least one artificially produced peptide and at least one reducing sugar, wherein the at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein; and wherein upon heating the composition, after infusion into an edible protein mass, a Maillard reaction occurs within the edible protein mass.

31. An alternative meat product of claim 30, comprising two or more of said at least one artificially produced peptide.

32. The alternative meat product of claim 31, 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.

33. The alternative meat product of claim 31 or 32, 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.

34. The alternative meat product of any one of claims 31 to 33, comprising at least 5 of said at least one artificially produced peptide.

35. The alternative meat product of any one of claims 31 to 34, wherein said at least one artificially produced peptide is selected by- subjecting a test sample comprising at least one artificially produced peptide to Gas Chromatography Mass Spectroscopy (GC-MS) under conditions that allow formation and extraction of odorants from the test sample; and- selecting the at least one artificially produced peptide as suitable for use in said composition, when said odorants correlate with volatile compounds derived from Maillard reaction in animal derived meat.

36. The alternative meat product of claim 35, wherein correlation is determined based on at least one parameter of gas chromatography and / or on odor activity value equal or greater than 1.

37. The alternative meat product of claim 35 or 36, wherein said at least one artificially produced peptide is selected when it correlates with at least 5 volatile compounds derived from Maillard reaction in animal derived meat.

38. The alternative meat product of any one of claims 31 to 37, 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.

39. The alternative meat product of any one of claims 31 to 38, wherein said at least one artificially produced peptide comprises between 5 and 20 amino acids.

40. The alternative meat product of any one of claims 31 to 39, wherein said at least one artificially produced peptide comprises between 7 and 18 amino acids.

41. The alternative meat product of any one of claims 31 to 40, wherein said 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, Pafl / RNA polymerase II complex component, synemin, SYNPO2, nebulin, troponin I, troponin T, titin, dystrophin, tropomyosin, myogenin, creatine kinase M-type, glyceraldehyde-3 -phosphatase dehydrogenase, carbonic anhydrase 3, Phosphoglycerate kinase 1, beta-enolase and myoglobin.

42. The alternative meat product of any one of claims 31 to 41, wherein said skeletal muscle protein is nebulin.

43. The alternative meat product of any one of claims 31 to 42, wherein said skeletal muscle protein is troponin.

44. The alternative meat product of any one of claims 31 to 43, wherein said skeletal muscle protein is creatine kinase M-type.

45. The alternative meat product of any one of claims 31 to 44, wherein said skeletal muscle protein is glyceraldehyde-3 -phosphatase dehydrogenase.

46. The alternative meat product of any one of claims 31 to 45, comprising at least one artificially produced peptide that corresponds to a hydrolysate of nebulin, at least one artificially produced peptide that corresponds to a hydrolysate of troponin, at least one artificially produced peptide that corresponds to a hydrolysate of creatine kinase M-type,and at least one artificially produced peptide that corresponds to a hydrolysate of glyceraldehyde-3 -phosphatase dehydrogenase.

47. The alternative meat product of any one of claims 31 to 46, comprising at least one additional artificially produced peptide that corresponds to a hydrolysate of a protein selected from the group consisting of Synaptotagmin binding cytoplasmic RNA interacting protein.

48. The alternative meat product of any one of claims 31 to 47, wherein said at least one artificially produced peptide is in a salt form.

49. The alternative meat product of any one of claims 31 to 48, comprising at least one artificially produced peptide comprises or consists of an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO:39 and / or an amino acid sequence having at least 80% identity with an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO:39, and capable of participating in a Maillard reaction once infused into and heated with an edible protein mass, in the presence of at least one reducing sugar.

50. The alternative meat product of any one of claims 31 to 49, comprising between about 5 and 39 of said at least one artificially produced peptide.

51. The alternative meat product of any one of claims 31 to 50, 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.

52. The alternative meat product of any one of claims 31 to 51, wherein said at least one reducing sugar comprises at least ribose.

53. The alternative meat product of any one of claims 31 to 52, comprising two or more reducing sugars.

54. The alternative meat product of any one of claims 31 to 53, wherein said at least one reducing sugar comprises ribose and dextrose.

55. The alternative meat product of any one of claims 31 to 54, comprising at least one amino acid monomer.

56. The alternative meat product of claim 55, wherein said at least one amino acid monomer is selected from the group consisting of glutathione, taurine, ornithine, carnosine, cystine, citrulline, P-alanine.

57. The alternative meat product of any one of claims 31 to 56, wherein said composition is infused into said edible protein mass.

58. The alternative meat product of any one of claims 31 to 57, wherein said edible protein mass comprises a plant protein.

59. The alternative meat product of claim 31, wherein said plant protein comprises texturized vegetable protein (TVP).

60. The alternative meat product of any one of claims 31 to 59, being animal free.

61. The alternative meat product of any one of claims 31 to 60, wherein said edible protein mass is in a form of a muscle scaffold.

62. A process of producing an alternative meat product comprising infusing an edible protein mass with a composition suitable for forming a Maillard reaction following heating of said alternative meat product, said composition comprises at least one artificially produced peptide and at least one reducing sugar, wherein the at least one artificially produced peptide corresponds to a hydrolysate of skeletal muscle protein .

63. The process of claim 62, wherein said infusing of the composition is by marination.

64. The process of claim 62 or 63, wherein said composition comprises two or more of said at least one artificially produced peptide.

65. The process of claim 64, 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.

66. The process of any one of claims 62 to 65, wherein said composition comprises at least 5 of said at least one artificially produced peptide.

67. The process of any one of claims 62 to 66, wherein said at least one artificially produced peptide in said composition is selected by- subjecting a test sample comprising at least one artificially produced peptide to Gas Chromatography Mass Spectroscopy (GC-MS) under conditions that allow formation and extraction of odorants from the test sample; and- selecting the at least one artificially produced peptide as suitable for use in said composition, when said odorants correlate with volatile compounds derived from Maillard reaction in animal derived meat.

68. The process of claim 67, wherein correlation is determined based on at least one parameter of gas chromatography and / or on odor activity value equal or greater than 1.

69. The process of claim 67 or 68, wherein said at least one artificially produced peptide is selected when it correlates with at least 5 volatile compounds derived from Maillard reaction in animal derived meat.

70. The process of any one of claims 62 to 69, 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.

71. The process of any one of claims 62 to 70, wherein said at least one artificially produced peptide comprises between 5 and 20 amino acids.

72. The process of any one of claims 62 to 71, wherein said at least one artificially produced peptide comprises between 7 and 18 amino acids.

73. The process of any one of claims 62 to 72, wherein said 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, Pafl / RNA polymerase II complex component, synemin, SYNPO2, nebulin, troponin I, troponin T, titin, dystrophin, tropomyosin, myogenin, creatine kinase M-type, glyceraldehyde-3 -phosphatase dehydrogenase, carbonic anhydrase 3, Phosphoglycerate kinase 1, beta-enolase and myoglobin.

74. The process of any one of claims 62 to 73, wherein said skeletal muscle protein is nebulin.

75. The process of any one of claims 62 to 73, wherein said skeletal muscle protein is troponin.

76. The process of any one of claims 62 to 73, wherein said skeletal muscle protein is creatine kinase M-type.

77. The process of any one of claims 62 to 73, wherein said skeletal muscle protein is glyceraldehyde-3 -phosphatase dehydrogenase.

78. The process of any one of claims 62 to 77, wherein said composition comprises at least one of said at least one artificially produced peptide that corresponds to a hydrolysate of nebulin, at least one of said at least one artificially produced peptide that corresponds to a hydrolysate of troponin, at least one of said at least one artificially produced peptide that corresponds to a hydrolysate of creatine kinase M-type, and at least one of said at least one artificially produced peptide that corresponds to a hydrolysate of glyceraldehyde-3 -phosphatase dehydrogenase.

79. The process of any one of claims 62 to 78, wherein said composition comprises at least one additional artificially produced peptide that corresponds to a hydrolysate of a protein selected from the group consisting of Synaptotagmin binding cytoplasmic RNA interacting protein.

80. The process of any one of claims 62 to 79, wherein said at least one artificially produced peptide is in a salt form.

81. The process of any one of claims 62 to 80, wherein said composition comprises at least one artificially produced peptide comprises or consists of an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO:39 and / or an amino acid sequence having at least 80% identity with an amino acid sequence as depicted in any one of SEQ ID NO: 1 to SEQ ID NO:39, and capable of participating in a Maillard reaction once infused into and heated with an edible protein mass, in the presence of at least one reducing sugar.

82. The process of any one of claims 62 to 81, wherein said composition comprises between about 5 and 39 of said at least one artificially produced peptide.

83. The process of any one of claims 62 to 82, wherein said at least one reducing sugar of said composition is selected from the group consisting of glucose, glucose-6 phosphate, galactose, fructose, ribose, maltose, glyceraldehyde, xylose, cellobiose, lactose.

84. The process of any one of claims 62 to 83, wherein said at least one reducing sugar of said composition comprises at least ribose.

85. The process of any one of claims 62 to 51, wherein said composition comprises two or more reducing sugars.

86. The process of any one of claims 62 to 85, wherein said at least one reducing sugar of said composition comprises ribose and dextrose.

87. The process of any one of claims 62 to 86, wherein said composition comprises at least one amino acid monomer.

88. The process of claim 87, wherein said at least one amino acid monomer is selected from the group consisting of glutathione, taurine, ornithine, carnosine, cystine, citrulline, P-alanine.

89. The process of any one of claims 62 to 88, wherein said edible protein mass comprises a plant protein.

90. The process of claim 89, wherein said plant protein comprises texturized vegetable protein (TVP).

91. The process of any one of claims 62 to 90, wherein said edible protein mass and said composition are animal free.

92. The process of any one of claims 62 to 91, wherein said edible protein mass is in a form of a muscle scaffold.

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