Structural Analysis of a Novel Aspartic-Type Endopeptidase from Moringa oleifera Seeds and Its Milk-Clotting Properties
文献类型： 外文期刊
作者： Wang, Xuefeng 1 ; He, Li 1 ; Zhao, Qiong 1 ; Shi, Yanan 1 ; Chen, Yue 2 ; Huang, Aixiang 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 650205, Yunnan, Peoples R China
关键词： Moringa oleifera seeds; aspartic-type endopeptidase; kappa-casein; cleavage site; flocculation reaction
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）
ISSN： 0021-8561
年卷期： 2021 年 69 卷 26 期
页码：
收录情况： SCI
摘要： A novel aspartic-type endopeptidase was previously obtained from Moringa oleifera seeds; however, its specific milk-clotting properties have remained unclear. Here, we used various biophysical and molecular simulation approaches for characterizing the structure and function of the aspartic-type endopeptidase. The endopeptidase was preferentially active toward kappa-casein (CN) and hydrolyzed it more than calf rennet; however, its ability to hydrolyze alpha-CN and beta-CN was weaker than that of calf rennet. The endopeptidase cleaved kappa-CN at Gln135-Asp136 and generated a 15 588.18 Da peptide with 135 amino acids. We further simulated the docking complex of the endopeptidase and kappa-CN and found out that they possibly combined with each other via hydrogen bonds. The flocculation reaction between the endopeptidase and kappa-CN indicated that milk coagulation occurred within 60 min. Overall, our observations suggest that the aspartic-type endopeptidase can be a potential rennet alternative for cheese making.
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