atuВестник Алматинского технологического университетаThe Journal of Almaty Technological University2304-568X2710-0839АО "АТУ"10.48184/2304-568X-2020-3-67-73atu-17Research ArticleТЕХНОЛОГИЯ ПИЩЕВОЙ И ПЕРЕРАБАТЫВАЮЩЕЙ ПРОМЫШЛЕННОСТИFOOD AND PROCESSING INDUSTRY TECHNOLOGYИсследование гидролизатов белков верблюжьих голяшек методом электрофореграммыResearch of camel shanks proteinhydrolyzates by electrophoregramСатаеваЖ. И.SatayevaZh. I.

Алматы

Almaty

julduz.kaynar@mai.ruТаеваА. М.TayevaA. M.

Алматы

Almaty

aigul_taeva@mail.ruАО «Алматинский технологический университет»Казахстан«Almaty Technological University» JSCKazakhstan202015012021036773Copyright © Сатаева Ж.И., Таева А.М., 20212021Сатаева Ж.И., Таева А.М.Satayeva Z.I., Tayeva A.M.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://atu.ejournal.kz/jour/article/view/17

Целью данного исследования является изучение степени гидролиза, определяющего при-роду гидролизатов белков, обусловливающих их размер и молекулярную массу методом электро-фореграммы. В этом исследовании использовалась суспензия поджелудочной железы верблюда для гидролиза белков из верблюжьих голяшек. Электрофорез в додецилсульфате натрия в полиакриламидном геле (SDS-PAGE) использовали для наблюдения за распределением белков и оценки их молекулярных масс в разное время инкубирования. Обработка электрофореграммы с помощью программы BioCapt (Vilber Lourmat, Франция) определяет характер гидролиза белка и пептидных профилей среди гидролизатов и время гидролиза в течение 8 часов показывает наибольшее накопление низкомолекулярных соединений с молекулярной массой <20 кДа, что является благоприятным результатом для потенциальной активности пептидов.

This research aims to study the degree of hydrolysis, determining the nature of protein hydrolyzates, which determine their size and molecular weight by the method of electrophoregram. In this research, a camel pancreas suspension was used to hydrolyze proteins from camel shanks. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to monitor the distribution of proteins and evaluate their molecular weights at different incubation times. Electrophoregram processing using the BioCapt program (Vilber Lourmat, France) determines the nature of the hydrolysis of protein and peptide profiles among hydrolyzates and the hydrolysis time for 8 hours shows the most significant accumulation of low molecular weight compounds with a molecular mass of <20 kDa, which is a favorable result for the potential activity of peptides.

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