ISSN 2074-9414 (Print),
ISSN 2313-1748 (Online)

Biomodification of Collagen-Containing By-Products by Enzymatic Hydrolysis

Low-value by-products can be processed using biotechnological methods, which seems to be the optimal solution for the problem of rational use of secondary raw materials. The authors introduce a method of biotransformation using whey and enzyme preparation of proteolytic action with subsequent massaging. The method neutralizes the specific smell, reduces the time of heat treatment, increases hydrophilicity, and reduces the mechanical strength of mutton rumen tissue. The experiment proved that the enzymatic effect on the connective tissue of the mutton rumen contributes to the destruction of disulfide and hydrogen bonds of the triple helix of the collagen macromolecule. It significantly reduces the mechanical strength and hydrothermal stability of collagen, which, in its turn, reduces the heat treatment time while increasing the functional and technological properties. The research revealed an increase in collagen digestibility. After 4 hours of fermentation, it was 4.5%, after 6 hours – 5.9%, and after 8 hours – 5.9%. Hence, the optimal period of fermentation was determined as 6 hours, since between 6 and 8 hours the main physical and chemical parameters improved insignificantly. The experiment in the cutting pressure of the raw lamb rumen tissue demonstrated softening of the structure as a result of the effect of the acidic medium on the collagen structure. An excess positive charge formed due to the suppression of dissociation of carboxyl groups of side chains. The loosening of the collagen structure occurred due to the expansion of fibrils in the polar areas, which can be attributed to the repulsion between similarly charged groups. As a result, the brine penetrated into the expanded area and caused swelling. The use of whey and fermentation contributed to an additional increase in moisture-binding and moisture-holding capacity. It loosened the structure of proteins and, thus, increased the degree of penetration and the immobilized moisture in the rumen. As a result, its mass increased by 10–20%, and the heat loss reduced. The composition of the brine contributed to the swelling, increased the diameter of the collagen fibers, and enlarged the surface of interaction in during massaging. Moisture was allowed to enter freely, which increased the water binding capacity by 22.2 ± 0.31%. The increase in the water binding capacity could be explained by the modification of collagen and its destructive changes. The changes occurred due to the additional interaction of whey molecules with the protein and the formation of new intermolecular bonds. Fermentation, combined with the massaging of the tripe, contributed to the development of lactic microflora and hydrolytic decomposition of protein components, thereby reducing the heat treatment process. Such changes are associated not only with the processes of protein hydrolysis under enzyme preparation, but also with the complex activity of lactic acid bacteria, as well as endo- and exoenzymes that hydrolyze proteins. The changes can also be attributed to the fact that low-molecular protein substances can assimilate and contribute to bacterial growth. In addition, lactic acid reduces the pH of the medium, thus activating the enzymatic properties. The proposed method of biotransformation of collagen-containing raw materials makes it possible to create environmentally friendly and low-waste technologies.
Collagen-containing raw materials, enzyme preparations, biotransformation, whey, functional products
  1. ‘Osnovy gosudarstvennoy politiki RF v oblasti zdorovogo pitaniya naseleniya na period do 2020 goda’ [‘Basic State Policy of the Russian Federation in the field of healthy nutrition for the period up to 2020’].
  2. Tekhnicheskiy reglament Tamozhennogo soyuza ‘O bezopasnosti myasa i myasnoy produktsii’ (TR TS 034/2013) [Technical regulations of the Customs Union ‘On the security of meat and meat products’ (TR CU 034/2013)] [Internet]. [cited 2018 May 14]. Available from:
  3. Tekhnicheskiy reglament Tamozhennogo soyuza ‘O bezopasnosti pishchevoy produktsii’ (TR TS 021/2011) [Technical regulations of the Customs Union ‘On food product safety’ (TR CU 021/2011)] [Internet]. [cited 2018 May 14]. Available from:
  4. Tolkacheva AA, Cherenkov DA, Korneeva OS, Ponomarev PG. Enzymes of industrial purpose - review of the market of enzyme preparations and prospects for its development. Proceedings of the Voronezh State University of Engineering Technologies. 2017;79(4)(74):197–203. (In Russ.). DOI:
  5. Antipova LV. Fermentnye tekhnologii v razvitie otechestvennogo proizvodstva pererabatyvayushchikh otrasley APK [Enzyme technologies in the development of domestic production of the processing industries in the agro-industrial complex]. 'Perspektivnye fermentnye preparaty i biotekhnologicheskie protsessy v tekhnologiyakh produktov pitaniya i kormov' sbornik trudov konferentsii' ['Advantageous enzyme preparations and biotechnological processes in food and feed technologies': conference proceedings]; Moscow; 2016. Moscow: Russian Scientific-Research Institute of Food Biotechnology of Russian Agricultural Sciences Academy; 2016. p. 61–66. (In Russ.).
  6. Plakhotina MS, Neustroeva VN, Litvina LA. Mikrobnye fermentnye preparaty dlya zhivotnovodstva [Microbial enzyme preparations for animal husbandry]. ‘Problemy biologii i biotekhnologii’: sbornik trudov konferentsii nauchnogo obshchestva studentov i aspirantov biologo-tekhnologicheskogo fakulʹteta [‘Problems of Biology and Biotechnology’: Proceedings of the conference conducted by the scientific community of students and postgraduates of the Department of Biology and Technology]; 2017; Novosibirsk. Novosibirsk: Novosibirsk State Agrarian University; 2017. p. 166–170. (In Russ.).
  7. Yunusov EhSh, Ponomarev VYa, Karimov AZ, Bezzubova EV, Ezhkova GO. Ispolʹzovanie ehkzogennykh fermentnykh preparatov v tekhnologii myasnykh produktov [Exogenous enzyme preparations in the technology of meat products]. Bulletin of the Technological University. 2012;15(22):119–121. (In Russ.).
  8. United States Department of Agriculture. Agricultural Research Service. USDA National Nutrient Database for Standard Reference.
  9. Dragunova MM, Brehova VP. Method of secondary collagen - containing raw material processing using Clavispora Lusitaniae Y3723 yeast. Food Processing: Techniques and Technology. 2014;32(1):18–21. (In Russ.).
  10. Dragunova MM, Prosekov AYu, Milentyeva IS, Krieger OV, Linnik AI. The technology development forprocessing of the meat processing industry collagen-containing wastes into the functional feed additive. The Bulletin of KrasGAU. 2014;98(11):203–206.
  11. Li C-M, Zhong Z-H, Wan O-H, Zhao H, Gu H-F, Xiong S-B. Preparation and thermal stability of collagen from scales of grass carp (Ctenopharyngodon idellus). European Food Research and Technology. 2008;227. DOI: 008-0869-z.
  12. Wang L, An X, Xin Z, Zhao L, Hu Q. Isolation and characterization of collagen from the skin of deep-sea redfish (Sebastes mentella). Journal of Food Science. 2007;72(8);450–455. DOI:
  13. Nalinanon S, Benjakul S, Visessanguan W, Kishimura H. Tuna pepsin: characteristics and its use for collagen extraction from the skin of threadfm bream (Nemipterus spp.). Journal of Food Science. 2008;73(5):413–419. DOI: j.1750-3841.2008.00777.x.
  14. Zhang Y, Liu W, Li G, Shi B, Miao Y, Wu X. Isolation and partial characterization of pepsin- soluble collagen from the skin of grass carp (Ctenopharyngodon idella). Food Chemistry. 2007;103(3):906–912. DOI: foodchem.2006.09.053.
How to quote?
Giro TM, Zybov SS, Yashin AV, Giro AV, Preobrazhensky VA. Biomodification of Collagen-Containing By-Products by Enzymatic Hydrolysis. Food Processing: Techniques and Technology. 2019;49(2):262–269. (In Russ.). DOI:
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