mkgtuНовые технологии / New technologiesNew Technologies2072-09202713-0029МГТУ10.47370/2072-0920-2026-22-3-40-55mkgtu-901Research ArticleПИЩЕВЫЕ СИСТЕМЫ И БИОТЕХНОЛОГИЯ ПРОДУКТОВ ПИТАНИЯ И БИОЛОГИЧЕСКИ АКТИВНЫХ ВЕЩЕСТВ (ТЕХНИЧЕСКИЕ НАУКИ)FOOD SYSTEMS AND BIOTECHNOLOGY OF FOOD AND BIOACTIVE SUBSTANCES (FOOD ENGINEERING)Антиоксидантные свойства гидролизатов куриного пераAntioxidant properties of chicken feather hydrolysateshttps://orcid.org/0000-0002-1687-9801БетехтинК. Э.BetekhtinK. E.

Бетехтин Кирилл Эдуардович – аспирант.

125080, Москва, Волоколамское шоссе, 11

Kirill E. Betekhtin - Postgraduate student, Russian Biotechnology University (ROSBIOTECH).

125080, Moscow, 11 Volokolamskoe Shosse

https://orcid.org/0009-0007-3781-4410БольшевН. А.BolshevN. A.

Большев Николай Алексеевич – магистрант.

125080, Москва, Волоколамское шоссе, 11

Nikolai A. Bolshev - Master student, Russian Biotechnology University (ROSBIOTECH).

125080, Moscow, 11 Volokolamskoe Shosse

nickolai.bolshev@yandex.ruhttps://orcid.org/0000-0002-5220-7877ЯдерецВ. В.YaderetsV. V.

Ядерец Вера Владимировна - кандидат биологических наук, доцент, доцент кафедры биотехнологии и биоорганического синтеза.

125080, Москва, Волоколамское шоссе, 11

Vera V. Yaderets - PhD (Biology), Associate Professor, the Department of Biotechnology and Bioorganic Synthesis, Russian Biotechnology University (ROSBIOTECH).

125080, Moscow, 11 Volokolamskoe Shosse

https://orcid.org/0000-0002-9287-0585МашенцеваН. Г.MashenzevaN. G.

Машенцева Наталья Геннадьевна - доктор технических наук, профессор, профессор РАН, профессор кафедры биотехнологии и биоорганического синтеза.

125080, Москва, Волоколамское шоссе, 11

Natalya G. Mashenzeva - Dr Sci. (Eng.), Professor, the Russian Academy of Sciences, Professor of the Department of Biotechnology and Bioorganic Synthesis, Russian Biotechnology University (ROSBIOTECH).

125080, Moscow, 11 Volokolamskoe Shosse

Федеральное государственное бюджетное образовательное учреждение высшего образования «Российский биотехнологический университет (РОСБИОТЕХ)»РоссияRussian Biotechnology University (ROSBIOTECH)Russian Federation2026131020262234055Copyright © Бетехтин К.Э., Большев Н.А., Ядерец В.В., Машенцева Н.Г., 20262026Бетехтин К.Э., Большев Н.А., Ядерец В.В., Машенцева Н.Г.Betekhtin K.E., Bolshev N.A., Yaderets V.V., Mashenzeva N.G.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://newtechology.mkgtu.ru/jour/article/view/901

Цель. Исследование антиоксидантных свойств пептидов, полученных при микробиологической ферментации перьевых отходов кератинолитическими штаммами Bacillus licheniformis БАЛ-1 и БАЛ-2. Методы. Мажорные пептидные последовательности (17 идентифицированных методом ЖХ-МС/МС с относительным содержанием >1 %) анализировали в базе BIOPEP-UWM для прогнозирования биоактивных профилей. Взаимодействие перспективных пептидов с Kelch-доменом белка Keap1 (PDB ID: 2FLU) оценивали методами молекулярного докинга (HPEPDOCK 2.0) и расчета термодинамических параметров комплексов (PRODIGY). Экспериментальную оценку общей антиоксидантной емкости (ОАЕ) гидролизатов проводили методами FRAP, DPPH и ORAC. Результаты. По данным in silico-анализа, большинство исследованных пептидов содержали фрагменты с прогнозируемой антиоксидантной активностью и формировали стабильные комплексы с Keap1. Наибольшую аффинность показал пептид GGGDIPRQPLYPPLPPRPG, для которого рассчитаны ΔG = -9,8 ккал·моль⁻¹ и Kd = 6,6×10⁻⁸ М; данный пептид взаимодействовал с ключевыми остатками связывающего центра (GLU216, ARG146, GLN239), конкурируя с эндогенным лигандом Nrf2. В тестах FRAP и DPPH активность образцов находилась ниже предела обнаружения, что обусловлено дефицитом реакционноспособных аминокислот (Cys, Trp) в пептидных фракциях, тогда как по методу ORAC гидролизаты БАЛ-1 и БАЛ-2 превосходили исходное перо в 25,5 и 31,3 раза, достигая значений 812,68±32,62 и 997,46±66,04 мкмоль-экв. кверцетина/л соответственно. Заключение. Полученные результаты подтверждают перспективность ферментированных гидролизатов куриного пера как источника биоактивных пептидов с двойным механизмом антиоксидантного действия (прямое гашение радикалов и активация Nrf2-пути) для дальнейшей разработки функциональных кормовых добавок. Практическая значимость работы заключается в обосновании возможности использования полученных гидролизатов в качестве компонента функциональных кормовых добавок для повышения резистентности сельскохозяйственной птицы к факторам окислительного стресса, что позволит снизить зависимость отрасли от синтетических антиоксидантов.

The goal of the research was to study the antioxidant properties of peptides obtained during microbiological fermentation of feather waste with keratinolytic strains of Bacillus licheniformis BAL-1 and BAL-2. The methods. The major 17 peptide sequences identified by LC-MS/MS with a relative content of >1% were analyzed in the BIOPEP-UWM database to predict bioactive profiles. The interaction of promising peptides with the Kelch domain of the Keap1 protein (PDB ID: 2FLU) was assessed using molecular docking (HPEPDOCK 2.0) and calculation of the thermodynamic parameters of the complexes (PRODIGY). Experimental assessment of the total antioxidant capacity (TAC) of the hydrolysates was performed using the FRAP, DPPH, and ORAC methods. The results. According to the in silico -analysis, most of the studied peptides contained fragments with the predicted antioxidant activity and formed stable complexes with Keap1. The highest affinity was demonstrated by the GGGDIPRQPLYPPLPPRPG peptide, for which ΔG = -9.8 kcal mol⁻¹ and Kd = 6.6×10⁻⁸ M were calculated; this peptide interacted with the key residues of the binding site (GLU216, ARG146, GLN239), competing with the endogenous ligand Nrf2. In the FRAP and DPPH tests, the activity of the samples was below the detection limit, which was due to the deficiency of reactive amino acids (Cys, Trp) in the peptide fractions. Whereas, according to the ORAC method, the BAL-1 and BAL-2 hydrolysates exceeded the original feather by 25.5 and 31.3 times, reaching values of 812.68±32.62 and 997.46±66.04 μmol-eq. quercetin/L, respectively. Conclusion. The obtained results confirm the potential of fermented chicken feather hydrolysates as a source of bioactive peptides with a dual mechanism of antioxidant action (direct radical scavenging and Nrf2 pathway activation) for the further development of functional feed additives. The practical significance of the research lies in substantiating the possibility of using the obtained hydrolysates as a component of functional feed additives to enhance the resistance of poultry to oxidative stress factors, thereby reducing the dependence of the industry on synthetic antioxidants.

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