References

meat

Theory and practice of meat processing

Теория и практика переработки мяса

2414-438X2414-441X

ФГБНУ «Федеральный научный центр пищевых систем им. В.М. Горбатова» РАН

10.21323/2414-438X-2019-4-4-12-16

meat-124

Research Article

Статьи

Biologically active peptides of meat and meat product proteins: a review. Part 1. General information about biologically active peptides of meat and meat products

Chernukha

I. M.

Irina M. Chernukha — doctor of technical sciences, professor, corresponding member to the Russian Academy of Sciences, leading research scientist, Experimental clinic-laboratory «Biologically active substances of an animal origin», 109316, Moscow, Talalikhina str., 26. Tel: +7–495–676–63–21

imcher@inbox.ru

Mashentseva

N. G.

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

natali-mng@yandex.ru

Afanasev

D. A.

Dmitrii A. Afanas’ev — student, Institute of Innovative Technologies and Bioindustry of Food Products, 125080, Moscow, Volokolamskoe sh., 11. Tel.: +7–985–456–77–82

dmitr.afanasjew2010@yandex.ru

Vostrikova

N. L.

Natal’ya L. Vostrikova — candidate of technical sciences, head of laboratory «Scientific and methodical work, biological and analytical research», 109316, Moscow, Talalikhina str., 26. Tel.: +7–495–676–79–81

vostrikova@fncps.ru

V.M. Gorbatov Federal Research Center for Food Systems of the Russian Academy of SciencesRussian FederationMoscow state university of food productionRussian Federation

2019

26122019

441216

2019

Chernukha I.M., Mashentseva N.G., Afanasev D.A., Vostrikova N.L.

Данная работа распространяется под лицензией Creative Commons Attribution 4.0.

This work is licensed under a Creative Commons Attribution 4.0 License.

https://www.meatjournal.ru/jour/article/view/124

Over many years, proteins and polypeptides have aroused scientific-practical interest due to multiple functions in the metabolic processes in the body upon vital activities. Biologically active substances of protein origin have wide application in different industries, including the food industry and medicine. At present, many studies are directed towards investigation of mechanisms of formation of such physiologically valuable food components as biologically active peptides and methods of their recovery from meat raw materials and meat products. A large part of literature data confirms that mechanisms of formation of such peptides are similar irrespective of methods of their generation. Their basis is enzymatic hydrolysis of muscle tissue proteins under the action of intracellular enzymes during autolysis, digestive enzymes of the human gastrointestinal tract or commercial enzyme preparations used in laboratories or in the industry. The method of culinary and/or technological processing also affects the process of biopeptide formation in meat products, namely, their recovery and availability.

biologically active peptidesautolysis of meat raw materialsenzymatic treatment of muscle tissueACE-I

The study was financed by the grant of the Russian Scientific Foundation (Project No.16–16–10073).

References1

Sentandreu, M.A., Coulis, G., Ouali, A. (2002). Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends in Food Science and Technology, 13(12), 400–421. DOI: 10.1016/S0924–2244(02)00188–7

Toldrá, F., Aristoy, M.-C., Mora, L., Reig, M. (2012). Innovations in value-addition of edible meat by-products. Meat Science, 92(3), 290–296. DOI: 10.1016/j.meatsci.2012.04.004

Albenzio, M., Santillo, A., Caroprese, M., Malva, A.D., Marino, R. (2017). Bioactive Peptides in Animal Food Products. Review. Foods. 6(5), 35. DOI: 10.3390/foods6050035

Bauchart, C., Rémond, D., Chambon, C., Patureau Mirand, P., Savary-Auzeloux, I., Reynès, C., Morzel, M. (2006). Small peptides (<5 kDa) found in ready-to-eat beef meat. Meat Science, 74(4), 658–666. DOI: 10.1016/j.meatsci.2006.05.016

Fu, Y., Young, J.F., Therkildsen, M. (2017). Bioactive peptides in beef: Endogenous generation through postmortem aging. Meat Science, 123, 134–142. DOI: 10.1016/j.meatsci.2016.09.015

Zhang, W., Xiao, S., Ahn, D.U. (2013). Protein oxidation: Basic principles and implications for meat quality. Critical Reviews in Food Science and Nutrition, 53(11), 1191–1201. DOI: 10.1080/10408398.2011.577540

Arihara, K. (2006). Strategies for designing novel functional meat products. Meat Science, 74(1), 219–229. DOI: 10.1016/j.meatsci.2006.04.028

Katayama, K., Anggraeni, H.E., Mori, T., Ahhmed, A.M., Kawahara, S., Sugiyama, M., Nakayama, T, Maruyama, M., Muguruma, M. (2008). Porcine skeletal muscle troponin is a good source of peptides with angiotensin-I converting enzyme inhibitory activity and antihypertensive effects in spontaneously hypertensive rats. Journal of Agricultural and Food Chemistry, 56(2), 355–360. DOI: 10.1021/jf071408j

Escudero, E., Sentandreu, M.A., Arihara, K., Toldrá, F. (2010). Angiotensin I‑converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat. Journal of Agricultural and Food Chemistry, 58(5), 2895–2901. DOI: 10.1021/jf904204n

Escudero, E., Toldrá, F., Sentandreu, M.A., Nishimura, H., Arihara, K. (2012). Antihypertensive activity of peptides identiﬁed in the in vitro gastrointestinal digest of pork meat. Meat Science, 91(3), 382–384. DOI: 10.1016/j.meatsci.2012.02.007

Saiga, A., Tanabe, S., Nishimura, T. (2003). Antioxidant activity of peptides obtained from porcine myoﬁbrillar proteins by protease treatment. Journal of Agricultural and Food Chemistry, 51(12), 3661–3667. DOI: 10.1021/jf021156g

Arihara, K., Ohata, M. (2006). Functional Properties of Bioactive Peptides Derived from meat Proteins. In book: Advanced Technologies for Meat Processing, Publisher: CRC Press (Boca Raton). pp. 245–273.

Morimatsu, F., Ito, M., Budijanto, S., Watanabe, I., Furukawa, Y., Kimura, S. (1996). Plasma cholesterol-suppressing effect of papain-hydrolyzed pork meat in rats fed hypercholesterolemic diet. Journal of Nutritional Science and Vitaminology, 42(2), 145– 153. DOI: 10.3177/jnsv.42.145

Shimizu, M., Sawashita, N., Morimatsu, F., Ichikawa, J., Taguchi, Y., Ijiri, Y., Yamamoto, J. Antithrombotic papain-hydrolyzed peptides isolated from pork meat. Thrombosis Research, 123(3), 753–757. DOI: 10.1016/j.thromres.2008.07.005

Jang, A., Jo, C., Kang, K.-S., Lee, M. (2008). Antimicrobial and human cancer cell cytotoxic effect of synthetic angiotensin-converting enzyme (ACE) inhibitory peptides. Food Chemistry, 107(1), 327–336. DOI: 10.1016/j.foodchem.2007.08.036

Banerjee, P., Shanthi, C. (2012). Isolation of novel bioactive regions from bovine Achilles tendon collagen having angiotensin I-converting enzyme-inhibitory properties. Process Biochemistry, 47(12), 2335–2346. DOI: 10.1016/j.procbio.2012.09.012

Fu, Y., Young, J.F., Lokke, M.M., Lametsch, R., Aluko, R. E. Therkildsen, M. (2016). Revalorisation of bovine collagen as a potential precursor of angiotensin I‑converting enzyme (ACE) inhibitory peptides based on in silico and in vitro protein digestions. Journal of Functional Foods, 24, 196–206. DOI: 10.1016/j.jff.2016.03.026

Saiga, A., Iwai, K., Hayakawa, T., Takahata, Y., Kitamura, S., Nishimura, T., Morimatsu, F. (2008). Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate. Journal of Agricultural and Food Chemistry, 56(20), 9586–9591. DOI: 10.1021/jf072669w

Li, B., Chen, F., Wang, X., Ji, B., Wu, Y. (2007). Isolation and identiﬁcation of antioxidative peptides from porcine collagen hydrolysate by consecutive chromatography and electrospray ionization–mass spectrometry. Food Chemistry, 102(4), 1135–1143. DOI: 10.1016/j.foodchem.2006.07.002

Escudero, E., Mora, L., Fraser, P.D., Aristoy, M.-C., Toldrá, F. (2013). Identiﬁcation of novel antioxidant peptides generated in Spanish dry-cured ham. Food Chemistry, 138(2–3), 1282–1288. DOI: 10.1016/j.foodchem.2012.10.133

Xing, L.-J., Hu, Y.-Y., Hu, H.-Y., Ge, Q.-F., Zhou, G.-H., Zhang, W.-G. (2016). Puriﬁcation and identiﬁcation of antioxidative peptides from dry-cured Xuanwei ham. Food Chemistry, 194, 951–958. DOI: 10.1016/j.foodchem.2015.08.101

Broncano, J.M., Otte, J., Petrón, M.J., Parra, V., Timón, M.L. (2012). Isolation and identiﬁcation of low molecular weight antioxidant compounds from fermented «chorizo» sausages. Meat Science, 90(2), 494–501. DOI: 10.1016/j.meatsci.2011.09.015

Fu, Y., Young, J.F., Therkildsen, M. (2017). Bioactive peptides in beef: Endogenous generation through postmortem aging. Meat Science, 123, 134–142. DOI: 10.1016/j.meatsci.2016.09.015

Lafarga, T., Hayes, M. (2014). Bioactive peptides from meat muscle and by-products: Generation, functionality and application as functional ingredients. Meat Science, 98(2), 227–239. DOI: 10.1016/j.meatsci.2014.05.036

Korhonen, H., Pihlanto-Leppälä, A., Rantamäki, P., Tupasela, T. (1998). Impact of processing on bioactive proteins and peptides. Trends in Food Science and Technology, 9(8–9), 307–319. DOI: 10.1016/S0924–2244(98)00054–5

Leygonie, C., Britz, T.J., Hoffman, L.C. (2012). Impact of freezing and thawing on the quality of meat: Review. Meat Science, 91(2), 93–98. DOI: 10.1016/j.meatsci.2012.01.013

Adje E.; BaAdje, E.Y., Balti, R., Kouach, M., Guillochon, D., Nedjar-Arroume, N. (2011). α 67–106 of bovine hemoglobin: A new family of antimicrobial and angiotensin I-converting enzyme inhibitory peptides. European Food Research and Technology, 232(4), 637–646. DOI: 10.1007/s00217–011–1430-z

Bauchart, C., Morzel, M., Chambon, C., Mirand, P.P., Reynès, C., Buffière, C., Rémond, D. (2007). Peptides reproducibly released by in vivo digestion of beef meat and trout flesh in pigs. British Journal of Nutrition, 98(6), 1187–1195. DOI: 10.1017/S0007114507761810

Pihlanto, A., Korhonen, H. (2003). Bioactive peptides and proteins. Advances in Food and Nutrition Research, 47, 175–276. DOI: 10.1016/S1043–4526(03)47004–6

Cheung, I.W.Y., Nakayama, S., Hsu, M.N.K., Samaranayaka, A.G.P., Li-Chan, E.C.Y. (2009). Angiotensim-I converting enzyme inhibitory activity of hydrolysates from oat (Avena sativa) proteins by in silico and in vitro analyses. Journal of Agricultural and Food Chemistry, 57(19), 9234–9242. DOI: 10.1021/jf9018245

Lafarga, T., O’Connor, P., Hayes, M. (2015). In silico methods to identify meat-derived prolylendopeptidase inhibitors. Food Chemistry, 175, 337–343. DOI: 10.1016/j.foodchem.2014.11.150

Vercruysse, L., Van Camp, J., Smagghe, G. (2005). ACE inhibitory peptides derived from enzymatic hydrolysate of animal protein: A review. Journal of Agricultural and Food Chemistry, 53(21), 8106–8115. DOI: 10.1021/jf0508908

Lafarga, T., O’Connor, P., Hayes, M. (2014). Identification of novel dipeptidyl peptidase-IV and angiotensin-I-converting enzyme inhibitory peptides from meat proteins using in silico analysis. Peptides, 59, 53–62. DOI: 10.1016/j.peptides.2014.07.005

Di Bernardini, R., Mullen, A.M., Bolton, D., Kerry, J., O’Neill, E., Hayes, M. (2012). Assessment of the angiotensin-I-converting enzyme (ACE-I) inhibitory and antioxidant activities of hydrolysates of bovine brisket sarcoplasmic proteins produced by papain and characterisation of associated bioactive peptidic fractions. Meat Science, 90(1), 226–235. DOI: 10.1016/j.meatsci.2011.07.008

Database BIOPEP [Electronic resource: http://www.uwm.edu.pl/biochemia/index.php/en/biopep. For access to information resources require authorization. Access date 20.09.2019]

Kȩska, P., Stadnik, J. (2016).Porcine myofibrillar proteins as potential precursors of bioactive peptides — an in silico study. Food and Function, 7(6), с. 2878–2885. DOI: 10.1039/c5fo01631b

Chernukha, I.M., Mashentseva, N.G., Vostrikova, N.L., Kovalev, L.I., Kovaleva, M.A., Afanasev, D.A., Bazhaev, A.A. (2018). Generation of bioactive peptides in meat raw materials exposed to proteases of different origin. Sel’skokhozyaistvennaya biologiya, 53(6), 1247–1261. DOI: 10.15389/agrobiology.2018.6.1247rus (in Russian)

Christensen, L., Ertbjerg, P., Løje, H., Risbo, J., van den Berg, F.W.J., Christensen, M. (2013). Relationship between meat toughness and properties of connective tissue from cows and young bulls heat treated at low temperatures for prolonged times. Meat Science, 93(4), 787–795. DOI: 10.1016/j.meatsci.2012.12.001

Yu, T.-Y., Morton, J.D., Clerens, S., Dyer, J.M. (2017). Cooking-induced protein modiﬁcations in meat. Comprehensive Reviews in Food Science and Food Safety, 16(1), 141–159. DOI: 10.1111/1541–4337.12243

Stadnik, J., Keska, P. (2015). Meat and fermented meat products as a source of bioactive peptides. Acta Scientiarum Polonorum, Technologia Alimentaria, 14(3), 181–190. DOI: 10.17306/J.AFS.2015.3.19

Toldra, F. (2004). Dry. In book: Encyclopedia of Meat Sciences. Three-Volume Set Volume 1–3. Edited by Jensen, W.K., Carrick Devine, C., Dikeman, M. New York: Elsevier. pp. 360–365. ISBN: 978–0–12–464970–5

Kato, T., Matsuda, T., Tahara, T., Sugimoto, M., Sato, Y., Nakamura, R. (1994). Effects of Meat-conditioning and Lactic Fermentation on Pork Muscle Protein Degradation. Bioscience, Biotechnology, and Biochemistry, 58(2), 408–410. DOI: 10.1271/bbb.58.408

Mora, L., Gallego, M., Toldra, F. (2018). ACEI–Inhibitory peptides naturally generated in meat and meat products and their health relevance. Review. Nutrients, 10(9), 1259. DOI: 10.3390/nu10091259

Zamaratskaia, G., Li, S. (2017). Proteomics in meat science — current status and future. Theory and Practice of Meat Processing, 2(1), 18–26. DOI: 10.21323/2414–438X-2017–2–1–18–26 (in Russian)

Di Luca, A., Elia, G., Mullen, A.M., Hamill, R.M. (2013). Monitoring post mortem changes in porcine muscle through 2-D DIGE proteome analysis of Longissimus muscle exudate. Proteome Science, 11(1), 9. DOI: 10.1186/1477–5956–11–9

Chernukha, I.M., Kovalev, L.I., Mashentseva, N.G., Kovaleva, M.A., Vostrikova, N.L. (2019). Detection of protein aggregation markers in raw meat and finished products. Foods and Raw Materials, 7(1), 118–123. DOI: 10.21603/2308–4057–2019–1–118–123

Chernukha I. M., Mashentseva N. G., Afanasiev D. A., Laptev G. U., Ilina L. A. (2019). Study of the effect of cholesterol-lowering starter cultures in smoked sausages on the formation of bioactive peptides and lipid profile in triton-induced hyperlipidemic rats. The 60th International Meat Industry Conference MEATCON2019, 333,012049. DOI:10.1088/1755–1315/333/1/012049

The authors declare that there are no conflicts of interest present.