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At present, different methods are used to accumulate functional peptides in meat raw materials, including the use of spontaneous microflora during autolysis, the use of the microbial enzymes (the application of starter cultures) and the use of the non-microbial enzymes (enzymes of animals and plant origin). Each method has its own specific characteristics of an impact on raw materials, which requires their detail study. This paper examines an effect of spontaneous microflora of fermented meat products from horsemeat on formation of biologically active peptides. Using the T-RFLP analysis, it was established that in air dried and uncooked smoked sausages produced with the use of the muscle tissue of horsemeat as a raw material, a significant proportion of microflora was presented by lactic acid microorganisms. The highest content of lactic acid microflora was observed in sample 1 (52.45 %), and the least in sample 3 (29.62 %). Sample 2 had the medium percent content of microflora compared to samples 1 and 3 — 38.82 %. It is necessary to note that about 25 % of microflora was unculturable; i.e., it had metabolic processes but did not grow on culture media. In the samples, the representatives of Actinobacteria and Pseudomonadales were found. Pathogenic and conditionally pathogenic microflora was not detected. Not only quantitative but also qualitative changes were observed in the studied samples. For example, in samples 1 and 2, the fractions of amilo-1,6-glucosidase, fast-type muscle myosin-binding-protein C; glucose-6-phosphate isomerase; fast skeletal muscle troponin I, phosphoglycerate kinase, pyruvate kinase and skeletal muscle actin were found, which were absent or reduced in sample 3. Therefore, in the studied product, good preservation of the main spectra of muscle proteins was observed, and the identified fractions, apparently, can be sources of new functional peptides. Not only quantitative but also qualitative changes were observed in the studied samples. For example, in samples 1 and 2, the C-terminal fragments of the myosin heavy chain were found, which were absent in sample 3. Also, the significant content of myoglobin was revealed in samples 2 and 3, and the myosin light chain was found in sample 1. Therefore, in the studied product, good preservation of muscle proteins myosin and myoglobin, which can be a source of new functional peptides, was observed. Based on the results of tandem mass-spectrometry, the proteins and natural short peptides present in the analyzed extracts were identified by the obtained masses. They belonged mainly to different peptides of equine myoglobin. Also, we identified several fragments, among which fast skeletal muscle troponin T and muscle creatine kinase were found. The obtained materials can be regarded as an experimental basis for the directed impact of starter cultures with a possibility to predict the protein and peptide composition of a finished product including with the aim of obtaining biologically active peptides.

About the Authors

I. M. Chernukha
V.M. Gorbatov Federal Research Center for Food Systems of Russian Academy of Sciences
Russian Federation

Irina M. Chernukha — doctor of technical sciences, professor, corresponding members of RAS, Head of the scientific direction of the center.

109316, Moscow, Talalikhina str., 26, Tel.: +7–495–676–97–18

I. N. Nikonov
«BIOTROPH» Limited
Russian Federation

Il’ya N. Nikonov  — deputy director for research and development.

196650, St. Petersburg, Kolpino, Izhorsky factory, 45, lit. ДВ, теl.: +7–812–322–85–50

N. G. Mashentseva
Moscow state university of food production
Russian Federation

Natal’ya G. Mashentseva  — doctor of technical sciences, professor RAS,, head of the Department of Biotechnology and Technology of Products of Bioorganic Synthesis.

125080, Moscow, Volokolamskoe sh., 11, tel.: +7–499–811–00–03, ext. 6883

D. L. Klabukova
Institute of Applied Biochemistry and Mechanical Engineering «Biochimmash»
Russian Federation

Daria L. Klabukova  — candidat of biological sciences, senior re‑ search scientist of Department of technologies and products based on cell cultures OJS.

127299, Moscow, Clary Tcetkin str., 4, tel.: +7–495–459–06–64

D. A. Afanasev
Moscow state university of food production
Russian Federation

Dmitrii A. Afanasev — student, Institute of Innovative Technologies and Bioindustry of Food Products.

125080, Moscow, Volokolamskoe sh., 11, tel.: +7–985–456–77–82

L. I. Kovalyov
Federal Research Centre «Fundamentals of Biotechnology» of the Russian Academy of Sciences
Russian Federation

Leonid I. Kovalyov — doctor of biological sciences, leading research scientist of the biomedical research laboratory.

119071, Moscow, Leninsky prospekt, 33 bldg. 2, Phone: +7–495–952–58–86

L. А. Ilina
«BIOTROPH» Limited
Russian Federation

Larisa A. Ilina — candidat of biological sciences, head of laboratory.

196650, St. Petersburg, Kolpino, Izhorsky factory, 45, lit. DV, теl.: +7–812–322–85–50


1. Hood, L., Flores, M. (2012). A personal view on systems medicine and the emergence of proactive P4 medicine: predictive, preventive, personalized and participatory. New Biotechnology, 29 (6), 613–624.

2. Tutel’yan, V.А., Samsonov, М.А., Kaganov, B.S., Baturin, А.К., Sarafetdinov, H.H., Plotnikova, О.А., Pavluchkova, М.S. (2008). Card catalogue of dishes of dietary (curative and prophylactic) nutrition of the optimized composition. Practical guideline. М.: National association of clinical nutrition.— 448 p. ISBN 978–5–85597–105–7. (in Russian).

3. Tutel’yan V.А., Vyalkov A.I., Razumov A.N., Mikhailov V.I., Moskalenko K.A., Odinets A.G., Sbehzneva V.G., Sergeev V.N. (2010). Scientific foundations of healthy nutrition. М, Panorama. — 839 p. ISBN 978–5–86472–224–4. (in Russian).

4. Arihara, K. (2006). Strategies for designing novel functional meat products. Meat Science, 74, 219–229.

5. Shishkin, S.S., Kovalev, L.I., Kovaleva, M.A., Ivanov, A.V., Eremina, L.S., Sadykhov, E.G. (2014).The application of proteomic technologies for the analysis of muscle proteins of farm animals used in the meat industry (Review). Applied Biochemistry and Microbiology, 50, 453–465.

6. Olmedilla-Alonso, B., Jimenez-Colmenero, F., Sanchez-Muniz, F.J. (2013). Development and assessment of healthy properties of meat and meat products designed as functional foods. Meat Science, 95, 919–930.

7. Te Pas, M.F.W, Kruijt, L., Pierzchala, M., Crump, R.E., Boeren, S., Keuning, E., Hoving-Bolink, R., Hortos, M., Gispert, M., Arnau, J., Diestre, A., Mulder, H.A. (2013). Identification of proteomic biomarkers in M. Longissimusdorsi as potential predictors of pork quality. Meat Science, 95, 679–687.

8. Yu, T. — Y., Morton, J.D., Clerens, S., Dyer, J.M. (2015). Proteomic Investigation of Protein Profile Changes and Amino Acid Residue Level Modification in Cooked Lamb Meat: The Effect of Boiling. Journal of Agricultural and Food Chemistry, 63(41), 9112–9123.

9. Chalamaiah, M., Jyothirmayi, T., Diwan, P.V., Dinesh Kumar, B. (2015). Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeorohita) roe (egg) prepared by gastrointestinal proteases. Journal of Food Science and Technology, 2015, 52 (12), 8300–8307.

10. Meinert, L., Broge, E.H.D.L., Bejerholm, C., Jensen, K. (2016). Application of hydrolyzed proteins of animal origin in processed meat. Food Science and Nutrition, 4(2), 290–297.

11. Lafarga, T., Rai, D. K., O’Connor, P., Hayes, M. (2015). A bovine fibrinogen-enriched fraction as a source of peptides with in vitro renin and angiotensin-i-converting enzyme inhibitory activities. Journal of Agricultural and Food Chemistry, 63, 8676–8684.

12. Minkiewicz, P., Dziuba, J., Michalska, J. (2011). Bovine meat proteins as potential precursors of biologically active peptides — a computational study based on the BIOPEP database. Food Science and Technology International, 17, 39–45.

13. Gobbetti, M., Minervini, F., Rizzello, C.G. (2004). Angiotensin I-converting-enzyme-inhibitory and antimicrobial bioactive peptides. International Journal of Dairy Technology, 57, 172–188.

14. Korhonen, H., Pihlanto, A. (2003). Food-derived bioactive peptides — Opportunities for designing future foods. Current Pharmaceutical Design, 9, 1297–1308.

15. Christensen, J.E., Dudley, E.G., Pederson, J.A., Steele, J.L. (1999). Peptidases and amino acid catabolism in lactic acid bacteria. Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology, 76, 217–246.

16. Doeven, M. K., Kok, J., Poolman, B. (2005). Specificity and selectivity determinants of peptide transport in Lactococcuslactis and other microorganisms. Molecular Microbiology, 57, 640–649.

17. Klaenhammer, T. R., Barrangou, R., Buck, B.L., Azcarate-Peril, M. A., Altermann, E. (2005). Genomic features of lactic acid bacteria effecting bioprocessing and health. FEMS Microbiology Reviews, 29, 393–409.

18. Savijoki K., Ingmer H., Varmanen P. (2006). Proteolytic systems of lactic acid bacteria. Applied Microbiology and Biotechnology, 71, 394–406.

19. Hébert, E. M., Mamone, G., Picariello, G., Raya, R. R., Savoy, G., Ferranti, P., Addeo, F. (2008). Characterization of the pattern of αs1- and β-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581. Applied and Environmental Microbiology, 74 (12), 3682–3689.

20. Hébert, E. M., Raya, R. R., de Giori G. S. (1999). Characterisation of a cell-envelope proteinase from Lactobacillus helveticus. Biotechnology Letters, 21(9), 831–834.

21. Hartmann, R., Meisel, H. (2007). Food-derived peptides with biological activity: from research to food applications. Current Opinion in Biotechnology, 18, 163–169.

22. Singh, V. P., Pathak, V., Verma, A. K. (2012). Fermented meat products: organoleptic qualities and biogenic amines–A review. American Journal of Food Technology, 7, 278–288.

23. Gaal, O., Medgyesi, G.A., Vereczkey, L. (1980). Electrophoresis in the Separation of Biological Macromolecules. Budapest, Akademiai Kiado.

24. Kovalyov, L.I., Shishkin, S.S., Kovalyova, M.A., Ivanov, A.V., Vostrikova, N.L., Chernukha, I.M. (2013). Proteomic research proteins in a sample of pork meat products. Vsyo o myase, 3, 32–34. (in Russian).

25. Kovalyov, L. I., Kovalyova, M. A., Kovalyov, P. L., Serebryakova, M. V., Moshkovskii, S. A., Shishkin, S.S. (2006). Polymorphism of Δ3,5-Δ2,4-dienoyl-coenzyme a isomerase (the ECH1 gene product protein) in human striated muscle tissue. Biochemistry (Moscow), 71(4), 448–453.

26. Zvereva, E.A., Kovalev, L.I., Ivanov, A.V., Kovaleva, M.A., Zherdev, A.V., Shishkin, S.S., Lisitsyn, A.B., Chernukha, I.M., Dzantiev, B.B. (2015). Enzyme immunoassay and proteomic characterization of troponin I as a marker of mammalian muscle compounds in raw meat and some meat products. Meat Science, 105 (1), 46–52.

For citation:

Chernukha I.M., Nikonov I.N., Mashentseva N.G., Klabukova D.L., Afanasev D.A., Kovalyov L.I., Ilina L.А. AN INFLUENCE OF SPONTANEOUS MICROFLORA OF FERMENTED HORSEMEAT PRODUCTS ON THE FORMATION OF BIOLOGICALLY ACTIVE PEPTIDES. Theory and practice of meat processing. 2017;2(4):4-19. (In Russ.)

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