期刊
LWT-FOOD SCIENCE AND TECHNOLOGY
卷 156, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.lwt.2021.113062
关键词
Binglangjiang buffalo; alpha-Glucosidase; Antidiabetic; Molecular docking; Dregea sinensis protease
资金
- Yunnan Province Major Science and Technology Special Program [202102AE090027]
- Yun-Ling Industrial Technology Leading Talent program [2014-1782]
In this study, novel alpha-glucosidase inhibitory peptides were isolated from buffalo milk. Four synthetic peptides were found to have alpha-glucosidase inhibitory activity, hindering the formation of complex and glycosylation between alpha-glucosidase and substrate. The study provides insights for understanding the antidiabetic mechanism of the peptides and the development of antidiabetic functional food.
Binglangjiang buffalo is a new type of river buffalo discovered in Tengchong of Yunnan Province, China, with rich protein in milk. In this study, we isolated novel alpha-glucosidase inhibitory peptides from the buffalo casein hydrolyzed by Dregea sinensis protease using RP-HPLC. A total of 26 peptides in the active fraction were identified by LC-MS/MS, mainly belonging to alpha(s1)-CN, alpha(s2)-CN, and beta-CN. Based on bioinformatics analysis, four peptides with potential alpha-glucosidase inhibitory activity were selected for chemical synthesis and activity verification. The four synthetic peptides exhibited alpha-glucosidase inhibitory activity and had IC(50)s of 470.492 +/- 3.086 mu mol/L (P3), 498.040 +/- 1.829 mu mol/L (P2), 503.635 +/- 3.269 mu mol/L (P1), and 542.502 +/- 1.995 mu mol/L (P4). Through molecular docking, we found that these four peptides may occupy the potential catalytic active sites (Arg387, Arg428, Arg727, Arg801, Arg799, and Trp710) of alpha-glucosidase through forming hydrogen bonds and hydrophobicity, thus hindering the formation of complex and glycosylation between alpha-glucosidase and substrate. Screening alpha-glucosidase from buffalo casein hydrolysates will provide insights for further study on the antidiabetic mechanism of the peptides and further development of antidiabetic functional food.
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