meatTheory and practice of meat processingТеория и практика переработки мяса2414-438X2414-441XФГБНУ «Федеральный научный центр пищевых систем им. В.М. Горбатова» РАН10.21323/2414-438X-2022-7-1-58-65meat-210Research ArticleСтатьиCertain features of using modified collagen-containing raw materials with prolonged shelf life in food technologyCertain features of using modified collagen-containing raw materials with prolonged shelf life in food technologyLitvinovaE. V.LitvinovaE. V.

Moscow

Elena V. Litvinova, Candidate of technical sciences, docent, Technology and Biotechnology of Meat and Meat Products Department

Talalikhina St., 33, 109396, Moscow

Tel.: +7–962–952–28–28

litvinovaev@mgupp.ruhttps://orcid.org/0000-0003-1821-7761TitovE. I.TitovE. I.

Moscow

Evgeny I. Titov, Doctor of technical sciences, professor, Academician of the Russian Academy of Sciences, Technology and Biotechnology of Meat and Meat Products Department

Talalikhina St., 33, 109396, Moscow

Tel.: +7–985–761–71–27

titov@mgupp.ruhttps://orcid.org/0000-0002-4089-2475KidyaevS. N.KidyaevS. N.

Moscow

Sergey N. Kidyaev, Candidate of technical sciences, docent, Technology and Biotechnology of Meat and Meat Products Department

Talalikhina St., 33, 109396, Moscow

Tel.: +7–985–150–81–91

kidaevsn@mgupp.ruhttps://orcid.org/0000-0001-7684-0557SokolovA. Yu.SokolovA. Yu.

Moscow

Alexander Yu. Sokolov, Candidate of technical sciences, docent, Department of Restaurant Business

Stremyanny lane, 36, Moscow, 117997

Tel.: +7–985–150–81–91

Sokolov.AY@rea.ruhttps://orcid.org/0000-0001-6749-7806LapshinaV. L.LapshinaV. L.

Moscow

Victoria L. Lapshina, assistant, Technology and Biotechnology of Meat and Meat Products Department

Talalikhina St., 33, 109396, Moscow

Tel.: +7–926–333–89–29

vic.toria.lapshina@inbox.ruMoscow State University of Food ProductionРоссияMoscow State University of Food ProductionRussian FederationPlekhanov Russian University of EconomicsРоссияPlekhanov Russian University of EconomicsRussian Federation202212042022715865Copyright © Litvinova E.V., Titov E.I., Kidyaev S.N., Sokolov A.Y., Lapshina V.L., 20222022Litvinova E.V., Titov E.I., Kidyaev S.N., Sokolov A.Y., Lapshina V.L.Litvinova E.V., Titov E.I., Kidyaev S.N., Sokolov A.Y., Lapshina V.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/210

In the current circumstances, trends in nutrition of a person striving to lead a healthy life-style require intake of meat products with the reduced energy value, minimal amounts of fat, increased protein mass fraction, presence of substances improving homeostasis of the body. The synergism of the modern nutrition science and meat industry enables creating food products that satisfy consumers’ demand. Today, in the Russian Federation, a theoretical and practical base of the technology development has been collected to the full extent in the field of rational processing of secondary raw materials in the food industry, optimal use of animal secondary raw materials, study of the protein ingredients of animal and plant origin and their deep scientifically substantiated processing, improvement of technological processes and equipment, and correspondently, product range extension. The paper broadens the information about the modified collagen-containing raw materials (cattle rumen), examines physico-chemical characteristics of the collagen-containing raw material and its changes in the process of freeze-drying with a special attention paid to the study of changes in the histological structure. The presence of the relatively uniform fibrillar structure was determined, which facilitated discovering the functional potential of proteinoids that form the fibrillar matrix in the composition of products from different groups. Analysis of IR-spectra revealed several significant absorption bands linked with the state of peptide bonds. The character of bands is linked with the complex of valence and deformation vibrations of the N- and С- types. It is believed that IR-spectra reflect conformations in the protein secondary structure, which suggests preserving properties of the tropocollagen particle or collagen molecule. Freeze-dried modified collagen-containing cattle rumen was tested by the example of jellies. The obtained databank broadens information about physico-chemical properties of modified collagen-containing raw materials (cattle rumen).

In the current circumstances, trends in nutrition of a person striving to lead a healthy life-style require intake of meat products with the reduced energy value, minimal amounts of fat, increased protein mass fraction, presence of substances improving homeostasis of the body. The synergism of the modern nutrition science and meat industry enables creating food products that satisfy consumers’ demand. Today, in the Russian Federation, a theoretical and practical base of the technology development has been collected to the full extent in the field of rational processing of secondary raw materials in the food industry, optimal use of animal secondary raw materials, study of the protein ingredients of animal and plant origin and their deep scientifically substantiated processing, improvement of technological processes and equipment, and correspondently, product range extension. The paper broadens the information about the modified collagen-containing raw materials (cattle rumen), examines physico-chemical characteristics of the collagen-containing raw material and its changes in the process of freeze-drying with a special attention paid to the study of changes in the histological structure. The presence of the relatively uniform fibrillar structure was determined, which facilitated discovering the functional potential of proteinoids that form the fibrillar matrix in the composition of products from different groups. Analysis of IR-spectra revealed several significant absorption bands linked with the state of peptide bonds. The character of bands is linked with the complex of valence and deformation vibrations of the N- and С- types. It is believed that IR-spectra reflect conformations in the protein secondary structure, which suggests preserving properties of the tropocollagen particle or collagen molecule. Freeze-dried modified collagen-containing cattle rumen was tested by the example of jellies. The obtained databank broadens information about physico-chemical properties of modified collagen-containing raw materials (cattle rumen).

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