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Peptidomic Analysis of Potential Bioactive Peptides in Mare Milk Under Different Heat Treatment Conditions

文献类型： 外文期刊

作者： Lou, Xiaoxiao 1 ; Shao, Wei 2 ; Wu, Yating 1 ; Ma, Hongpeng 1 ; Chen, He 1 ; Zheng, Nan 1 ; Zhao, Yankun 1 ;

作者机构： 1.Xinjiang Acad Agr Sci, Inst Qual Stand & Testing Technol Agroprod, Agr Prod Qual & Safety Risk Assessment Lab, Minist Agr & Rural Affairs Lab Qual & Safety Risk, Urumqi 830091, Peoples R China

2.Coll Anim Sci, Xinjiang Meat & Milk Herbivore Nutr Lab, Urumqi 830052, Peoples R China

3.Chinese Acad Agr Sci, Key Lab Qual & Safety Control Milk & Dairy Prod, Minist Agr & Rural Affairs, Inst Anim Sci, Beijing 100193, Peoples R China

关键词： mare milk; bioactive peptides; temperature stage; biological activity

期刊名称：FOODS （ 影响因子：5.1； 五年影响因子：5.6 ）

ISSN：

年卷期： 2024 年 13 卷 22 期

页码：

收录情况： SCI

摘要： Active peptides in mare milk have unique biological activities, but how the bioactive protein in mare's milk changes under the influence of temperature has not been fully studied. Therefore, in this study, the differential expression of bioactive peptides potentially present in horse milk under different heat treatment conditions was investigated for the first time using peptidomic and bioinformatic techniques. We collected a total of 15 samples. In this study, we divided the samples into five groups, specifically, 65 degrees C, 30 min; 72 degrees C, 15 min; 83 degrees C; 10 min; 95 degrees C, 5 min; and an untreated group as a control, which involved four different temperature treatments, in order to understand changes in bioactive peptides and to identify the sequence of bioactive peptides. In the experiment, a total of 2341 active peptides were identified. The amino acid composition of the potential active peptides remained stable across different temperatures, but their abundance varied with temperature. In all, 23 peptides from 20 different proteins were identified, with the highest number of active peptides identified at 72 degrees C. Through database searches, we found that a majority of these peptides were within beta-lactoglobulin and immunoglobulin domain proteins, which are known for their potential biological activities. These findings provide a theoretical foundation for the development of peptides with different bioactivities as potential functional foods.

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