Identification and characterization of DPP-IV inhibitory peptides from silver carp swim bladder hydrolysates

被引：58
作者：
Hong, Hui [1 ,3 ]
Zheng, Yanyan [1 ]
Song, Sijia [1 ]
Zhang, Yuqi [1 ]
Zhang, Chi [1 ]
Liu, Jun [2 ]
Luo, Yongkang [1 ]
机构：
[1] China Agr Univ, Coll Food Sci & Nutr Engn, Beijing 100083, Peoples R China
[2] Jiangxi Normal Univ, Natl Res & Dev Ctr Freshwater Fish Proc, Nanchang 330022, Jiangxi, Peoples R China
[3] China Agr Univ, Xinghua Ind Res Ctr Food Sci & Human Hlth, Xinghua 225700, Jiangsu, Peoples R China
来源：
FOOD BIOSCIENCE | 2020年 / 38卷
基金：
国家重点研发计划;
关键词：
Silver carp; Hypophthalmichthys molitrix; Swim bladder; DPP-IV inhibitory Peptide; Insulin secretion;
D O I：
10.1016/j.fbio.2020.100748
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
Dipeptidyl peptidase IV (DPP-IV) has an important role in blood glucose metabolism. Silver carp swim bladder protein was hydrolyzed using papain, bromelain, Alcalase 2.4 L, Neutrase, and Flavourzyme. The swim bladder hydrolysate obtained using 5 h hydrolysis of Neutrase showed the highest DPP-IV inhibition (81 +/- 2%) at 5 mg/mL. This hydrolysate was purified sequentially using ultrafiltration, gel filtration chromatography, and RP-HPLC. Peptide sequences from the RP-HPLC fractions were identified using liquid chromatography tandem mass spectrometry. The most potent DPP-IV inhibitory peptide WGDEHIPGSPYH (IC50: 0.35 +/- 0.01 mM) showed an uncompetitive inhibition mode. Docking analysis showed that the binding site of WGDEHIPGSPYH was located inside the cavity of the DPP-IV monomer, which was close to the catalytic site. WGDEHIPGSPYH and its hydrolysate IPGSPY were transported intact across a Caco-2 cell monolayer. These two peptides were tested for their effects on Caco-2 and INS-1 cells and both showed good inhibition for soluble DPP-IV and promoted insulin secretion.
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页数：10
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