Selection of Working Parameters for the Production of Egg Protein Peptides

Bolkhonov, B.A.; Sokolov, D.V.; Жамсаранова, С. Д.; Лебедева, С. Н.; Chen, Qian

doi:10.53980/24131997_2022_4_15

Cited by 3 publications

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“…The content of total nitrogen was determined with the help of Nessler's reagent according to GPM.1.7.2.0027. 15 1, the content of amine nitrogen in non-hydrolyzed raw materials and the resulting hydrolysates was determined by the method of formal titration (Sorens method) according to GPM.1.2.3.0022.15 2.…”

Section: Objects and Methodsmentioning

confidence: 99%

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Hydrolysate of ovalbumin: production and evaluation of the functional properties of peptides

Жамсаранова

Лебедева

Bolkhonov

et al. 2023

Teor. prakt. pererab. mâsa (Print)

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Chicken eggs proteins and their derivatives, like protein hydrolysates, peptides and amino acids, possess high nutritional value and provide a wide range of biological activity. They serve as sources for development of functional ingredients that draw the attention of specialists in the food production and biomedical industries, as well as the livestock feed industry. Enzymatic hydrolysis of proteins is a popular process for obtaining bioactive peptides with multifunctional properties. The purpose of this study is to obtain a hydrolysate of ovalbumin with a high degree of hydrolysis and to determine its functional and technological parameters. The research presents a two-stage scheme of ovalbumin hydrolysis with the help of pepsin and trypsin which provide high degree of hydrolysis (82-83%). The fractional composition of the hydrolysate is determined. The fractional composition is represented by three main fractions (high, medium and low molecular weight). The summarized antioxidant activity (SAA) of the hydrolysate is considered within the dynamics of the hydrolysis process. The highest SAA value was noted after 2 hours, and it amounted to 170.23 mg/l; at the end of hydrolysis the SAA value was equal to 114.31 mg/l. When analyzing the SAA, it was found that the main contribution to the summarized antioxidant activity of the ovalbumin hydrolysate is made by peptides of the medium molecular fraction. The microfiltration process, used in the research, made it possible to separate high-molecular compounds, which led to an increase in the SAA of the hydrolysate to 189.9 mg/l. The main functional and technological parameters of the hydrolysate are determined in this research. The comprehensive study of the biological activity and functional characteristics of egg protein hydrolysates and their peptides provides a theoretical basis for expanding the range of functional ingredients obtained from food proteins and for replenishing the range of functional foods.

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Section: Objects and Methodsmentioning

confidence: 99%

“…The research of the authors B. A. Bolkhonova et al is devoted to the selection of operable parameters for obtaining peptides of an egg white [15].…”

Section: Introductionmentioning

confidence: 99%

Hydrolysate of ovalbumin: production and evaluation of the functional properties of peptides

Жамсаранова

Лебедева

Bolkhonov

et al. 2023

Teor. prakt. pererab. mâsa (Print)

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Functional Profile of Enzymatic Hydrolysates in Food Proteins

Lebedeva,

Bolkhonov,

Zhamsaranova

et al. 2024

Food Processing: Techniques and Technology

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Food allergy is a matter of global concern, proteins being a popular allergen worldwide. Enzymatic protein hydrolysates serve as hypoallergenic components in functional foods. This article describes enzymatic hydrolysates of egg and soy proteins as potential antigens, sensitizers, and antioxidants. The research featured soy protein isolate and egg albumin. The protein hydrolysates were obtained in a two-step process with pepsin and trypsin to measure hydrolysis, total antioxidant activity, and residual antigenicity. The sensitizing ability of native proteins and their hydrolysates was studied using a delayed-type hypersensitivity (DTH) skin test of paw swelling in mice. The egg albumin and soy protein were hydrolyzed by sequentially adding the proteases, i.e., pepsin and trypsin. The degree of protein hydrolysis was calculated against total nitrogen and its contents in non-hydrolyzed raw materials and hydrolysate. It was 82.6% for the egg hydrolysate and 88.3% for the soy hydrolysate, the total antioxidant activity being 114.3 and 91.4 mg/100 mL, respectively. The residual antigenicity of the hydrolysates determined by ELISA in a sandwich version was 1.55×10–4 and 3.30×10–4 RU, respectively. The native egg and soy proteins demonstrated good allergenic properties, and the DTH response index increased fivefold. The hydrolysates reduced the DTH response indices by an average of 3.5 for egg hydrolysate and 2.6 times for soy hydrolysate. The resulting enzymatic hydrolysates of egg albumin and soy protein demonstrated a high degree of hydrolysis and antioxidant activity. They had low residual antigenicity (10–4) and low sensitizing ability. The resulting enzymatic hydrolysates could be used as hypoallergenic components and antioxidants in new functional foods.

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Математическое Моделирование Ферментации Белка Молозива Коров Для Получения Антимикробных И Противогрибковых Пептидов

Мерзлякова,

Тихонов,

Тихонова

et al. 2023

АПК России

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Настоящая статья посвящена разработке математической модели получения трипсинового гидролизата молозива коров с прогностическим функционалом оценки различных показателей биологической активности, в частности бактериостатической и противогрибковой активности, выделенного из него пептида. В ходе исследования были смоделированы режимы ферментолиза молозива коров для получения гидролизатов антимикробной направленности, после чего антимикробная активность полученного из гидролизата пептида была подтверждена в ходе экспериментальных исследований. Модельные значения частных оценочных критериев эффективности процесса гидролиза были установлены на уровне: продолжительность гидролиза (4–5 ч.), степень гидролиза (60 %), соотношение фермент:субстрат (1:17 %), pH (7,8) и t (39 °C). Для полученного и идентифицированного посредством базы данных Protein NCBI антимикробного пептида с условным названием Т1.2 в ходе эксперимента масс-спектрометрическим методом определена молекулярная масса (22 кДа), аминокислотная последовательность (28 аминокислот, последовательность STKRHRMHACSWRGPLKALSNPRAEFRR), а также методом молекулярного моделирования определены заряд (+7), изоэлектрическая точка (12,49) и гидрофильность (+31,07 Ккал·моль–1). Диско-диффузным методом проверена и доказана антимикробная активность в отношении бактериальных культур E. coli и B. subtilis, а также противогрибковая активность в отношении грибковой культуры C. Albicans. Выявлено, что активность Т1.2 существенно ниже по сравнению с действием антибиотика «Канамицин» и противогрибкового препарата «Флуканазол», при этом он может быть рекомендован как синергетик при стандартной протокольной терапии антибактериальными и противогрибковыми препаратами при условии доказательства его биодоступности и отсутствия токсичности.

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Selection of Working Parameters for the Production of Egg Protein Peptides

Cited by 3 publications

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Hydrolysate of ovalbumin: production and evaluation of the functional properties of peptides

Hydrolysate of ovalbumin: production and evaluation of the functional properties of peptides

Functional Profile of Enzymatic Hydrolysates in Food Proteins

Математическое Моделирование Ферментации Белка Молозива Коров Для Получения Антимикробных И Противогрибковых Пептидов

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