Protein function analysis of germinated Moringa oleifera seeds, and purification and characterization of their milk-clotting peptidase
文献类型： 外文期刊
作者： Wang, Xuefeng 1 ; He, Li 1 ; Zhao, Qiong 1 ; Chen, Haoran 1 ; Shi, Yanan 1 ; Fan, Jiangping 1 ; Chen, Yue 2 ; Huang, Aixi 1 ;
作者机构： 1.Yunnan Agr Univ, Coll Food Sci & Technol, Kunming 650201, Yunnan, Peoples R China
2.Yunnan Acad Agr Sci, Biotechnol & Germplasm Resources Inst, Kunming 650223, Yunnan, Peoples R China
关键词： Germinated Moringa oleifera seeds; Proteomics; Protein function; Milk-clotting activity; Cysteine peptidase
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：6.953； 五年影响因子：6.737 ）
ISSN： 0141-8130
年卷期： 2021 年 171 卷
页码：
收录情况： SCI
摘要： The present study aimed to investigate the biological functions of germinated M. oleifera seed proteins and to identify the identity of milk-clotting proteases. A total of 963 proteins were identified, and those with molecular weights between 10 and 30 kDa were most abundant. The identified proteins were mainly involved in energy-associated catalytic activity and metabolic processes, and carbohydrate and protein metabolisms. The numbers of proteins associated with the hydrolytic and catalytic activities were higher than the matured dry M. oleifera seeds reported previously. Of the identified proteins, proteases were mainly involved in the milk-clotting activity. Especially, a cysteine peptidase with a molecular mass of 17.727 kDa exhibiting hydrolase and peptidase activities was purified and identified. The identified cysteine peptidase was hydrophilic, and its secondary structure consisted of 27.60% alpha helix, 9.20% beta fold, and 63.20% irregular curl; its tertiary structure was also constructed using M. oleifera seed 2S protein as the protein template. The optimal pH and temperature of the purified protease were pH 4.0 and 60 degrees C, respectively. The protease had high acidic stability and good thermostability, thus could potentially be applied in the dairy industry. (C) 2021 Published by Elsevier B.V.
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