Dahiya, S. Food waste biorefinery: Sustainable strategy for circular bioeconomy / S. Dahiya, A.N. Kumar, J.S.S. Chatterjee [et al.] // Bioresource Technology. – 2018. – V. 248. – P. 2-12.
Министерство сельского хозяйства Российской Федерации. Об утверждении Ветеринарных правил перемещения, хранения, переработки и утилизации биологических отходов. Приказ № 626. Электронный ресурс. – Режим доступа: [https://www.mos.ru/moskomvet/documents/4/view/246457220/]. Дата обращения: 13.06.2023.
Ministerstvo sel'skogo khozyaystva Rossiyskoy Federatsii. Ob utverzhdenii Veterinarnykh pravil peremeshcheniya, khraneniya, pererabotki i utilizatsii biologicheskikh otkhodov. Prikaz № 626 [Ministry of Agriculture of the Russian Federation. On approval of the Veterinary Rules for the movement, storage, processing and disposal of biological waste. Order № 626]. Electronic resource. – Access mode: [https://www.mos.ru/moskomvet/documents/4/view/246457220/]. Date of access: 13.06.2023.
Ungureanu, N. Management of By-products and Waste from Poultry Meat Industry / N. Ungureanu, V. Vladut, S.-S. Biris [et al.] // International Journal of Engineering. – 2023. – V. 21. – № 1. – P. 165-174.
Alao, B. The Potential of Animal By-Products in Food Systems: Production, Prospects and Challenges / B. Alao, A. Falowo, A. Chulayo [et al.] // Sustainability. – 2017. – V. 9. – № 7. – P. 1089.
Marti, D.L. Where’s the (Not) Meat? Byproducts From Beef and Pork Production / D.L. Marti, R.J. Johnson, K.H.Jr. Mathews // LDP-M-209-01. – 2011.
Reguengo, L.M. Agro-industrial by-products: Valuable sources of bioactive compounds / L.M. Reguengo, M.K. Salgaço, K. Sivieri [et al.] // Food Research International. – 2022. – V. 152. – P. 110871.
Лукинова, Е.А. Антимикробные вещества: альтернативный подход к продлению сроков хранения / Е.А. Лукинова, Е.А. Котенкова, А.Н. Макаренко // Теория и практика переработки мяса. – 2017. – Т. 2. – № 3. – С. 4-20. DOI: 10.21323/2414-438X-2017-2-3-4-20.
Lukinova, Е.А. Antimicrobial substances: an alternative approach to the extension of shelf life / Е.А. Lukinova, Е.А. Kotenkova, А.N. Makarenko // Theory and practice of meat processing. – 2017. – T. 2. – № 3. – P. 4-20. DOI: 10.21323/2414-438X-2017-2-3-4-20.
Jeria, N. Beneficial Effects of Bioactive Compounds Obtained from Agro-Industrial By-Products on Obesity and Metabolic Syndrome Components / N. Jeria, S. Cornejo, G. Prado [et al.] // Food Reviews International. – 2022. – P. 1-30.
Patra, A. Review on the extraction of bioactive compounds and characterization of fruit industry by-products / A. Patra, S. Abdullah, R.C. Pradhan // Bioresources and Bioprocessing. – 2022. – V. 9. – № 1. – P. 14.
O’Shea, N. Dietary fibre and phytochemical characteristics of fruit and vegetable by-products and their recent applications as novel ingredients in food products / N. O’Shea, E.K. Arendt, E. Gallagher // Innovative Food Science & Emerging Technologies. – 2012. – V. 16. – P. 1-10.
Antimicrobial Peptide Database. Electronic resource. – Access mode: [https://aps.unmc.edu/]. Date of access: 31.05.2023.
Ryu, M. Rediscovery of antimicrobial peptides as therapeutic agents / M. Ryu, J. Park, J.-H. Yeom [et al.] // Journal of Microbiology. – 2021. – V. 59. – № 2. – P. 113-123.
Kotenkova, E. Bovine mucous membranes as a source of antimicrobial compounds / E. Kotenkova, E. Lukinova, L. Kovalyov // Potravinarstvo Slovak Journal of Food Sciences. – 2018. – V. 12. – № 1. – P. 667-672.
O’Farrell, P. High resolution two-dimensional electrophoresis of proteins / P. O’Farrell // Journal of Biological Chemistry. – 1975. – V. 250. – № 10. – P. 4007-4021.
Kovalyov, L.I. Polymorphism of Δ3,5-Δ2,4-dienoyl-coenzyme A isomerase (the ECH1 gene product protein) in human striated muscle tissue / L.I. Kovalyov, M.A. Kovalyova, P.L. Kovalyov [et al.] // Biochemistry. – 2006. – V. 71. – № 4. – P. 448-453.
Zvereva, E.A. Enzyme immunoassay and proteomic characterization of troponin I as a marker of mammalian muscle compounds in raw meat and some meat products / E.A. Zvereva, L.I. Kovalyov, A.V. Ivanov [et al.] // Meat Science. – 2015. – V. 105. – P. 46-52.
База данных «Протеомика мышечных органов». Электронный ресурс. – Режим доступа: [http://mp.inbi.ras.ru/index.php/]. Дата обращения: 21.06.2022.
Baza dannykh «Proteomika myshechnykh organov» [Database "Proteomics of muscular organs"]. Electronic resource. – Access mode: [http://mp.inbi.ras.ru/index.php/]. Date of access: 21.06.2022.
Dell’Angelica, E.C. Primary structure and binding properties of calgranulin C, a novel S100-like calcium-binding protein from pig granulocytes / E.C. Dell’Angelica, C.H. Schleicher, J.A. Santomé // The Journal of biological chemistry. – 1994. – V. 269. – № 46. – P. 28929-28936.
O95994 AGR2_HUMAN. Anterior gradient protein 2 homolog. Electronic resource. – Access mode: [https://www.uniprot.org/uniprotkb/O95994/entry/]. Date of access: 30.08.2022.
Wang, Z. The adenocarcinoma-associated antigen, AGR2, promotes tumor growth, cell migration, and cellular transformation / Z. Wang, Y. Hao, A.W. Lowe // Cancer Research. – 2008. – V. 68. – № 2. – P. 492-497.
Otto, M. Staphylococcus aureus toxins / M. Otto // Current Opinion in Microbiology. – 2014. – V. 17. – P. 32-37.
Calander, A.-M. Impact of staphylococcal protease expression on the outcome of infectious arthritis / A.M. Calander, I.M. Jonsson, A. Kanth [et al.] // Microbes and Infection. – 2004. – V. 6. – № 2. – P. 202-206.
Malanovic, N. Antimicrobial Peptides Targeting Gram-Positive Bacteria / N. Malanovic, K. Lohner // Pharmaceuticals. – 2016. – V. 9. – № 3. – P. 59.
Tossi, A. Amphipathic, α-helical antimicrobial peptides / A. Tossi, L. Sandri, A. Giangaspero // Peptide Science. – 2000. – V. 55. – № 1. – P. 4-30.
Xiao, B. Structure of mammalian AMPK and its regulation by ADP / B. Xiao, M.J. Sanders, E. Underwood [et al.] // Nature. – 2011. – V. 472. – № 7342. – P. 230-233.
Boparai, J.K. Mini Review on Antimicrobial Peptides, Sources, Mechanism and Recent Applications / J.K. Boparai, P.K. Sharma // Protein & Peptide Letters. – 2019. – V. 27. – № 1. – P. 4-16.
Kościuczuk, E.M. Cathelicidins: family of antimicrobial peptides. A review / E.M. Kościuczuk, P. Lisowski, J. Jarczak [et al.] // Molecular Biology Reports. – 2012. – V. 39. – № 12. – P. 10957-10970.
Wang, G. APD2: the updated antimicrobial peptide database and its application in peptide design / G. Wang, X. Li, Z. Wang // Nucleic Acids Research. – 2009. – V. 37. – № s1. – P. D933-D937.
Gruenheid, S. Resistance to antimicrobial peptides in Gram-negative bacteria / S. Gruenheid, H. Moual // FEMS Microbiology Letters. – 2012. – V. 330. – № 2. – P. 81-89.
Nikolaev, Y. Microbial Biofilms at Meat-Processing Plant as Possible Places of Bacteria Survival / Y. Nikolaev, Yu. Yushina, A. Mardanov [et al.] // Microorganisms. – 2022. – V. 10. – № 8. – P. 1583.
Ghafoor, A. Role of exopolysaccharides in Pseudomonas aeruginosa biofilm formation and architecture / A. Ghafoor, I.D. Hay, B.H.A. Rehm // Applied and environmental microbiology. – 2011. – V. 77. – № 15. – P. 5238-5246.
Jakobsen, T. Bacterial Biofilm Control by Perturbation of Bacterial Signaling Processes / T. Jakobsen, T. Tolker-Nielsen, M. Givskov // International Journal of Molecular Sciences. – 2017. – V. 18. – № 9. – P. 1970.
Malik, E. pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents / E. Malik, S. Dennison, F. Harris [et al.] // Pharmaceuticals. – 2016. – V. 9. – № 4. – P. 67.
Пантелеев, П.В. Строение и биологические функции β-шпилечных антимикробных пептидов / П.В. Пантелеев, И.А. Болосов, С.В. Баландин [и др.] // Acta Naturae. – 2015. – Т. 7. – № 1. – С. 39-50.
Panteleev, P.V. Structure and biological functions of β-hairpin antimicrobial peptides / P.V. Panteleev, I.А. Bolosov, S.V. Balandin [et al.] // Acta Naturae. – 2015. – V. 7. – № 1. – P. 39-50.