文献类型：期刊文献

英文题名：Purification, identification and molecular mechanism of two dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from Antarctic krill (Euphausia superba) protein hydrolysate

作者：Ji, Wei[1];Zhang, Chaohua[2,3,4];Ji, Hongwu[2,3,4]

机构：[1]Guangzhou Univ Educ, Coll Biol & Food Engn, Guangzhou 510303, Guangdong, Peoples R China;[2]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China;[3]Guangdong Prov Key Lab Aquat Prod Proc & Safety, Zhanjiang 524088, Peoples R China;[4]Guangdong Higher Educ Inst, Key Lab Adv Proc Aquat Prod, Zhanjiang 524088, Peoples R China

年份：2017

卷号：1064

起止页码：56

外文期刊名：JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES

收录：SCI-EXPANDED(收录号：WOS:000412958100009)、、WOS

基金：This work was supported by the Modern Agro-industry Technology Research System of China (grant number CARS-47); Discipline Construction Project of Institutions of Higher Learning in Guangdong Province of China (grant number 2013CXZDA020); Guangdong Ocean University Strong School Innovation Fund Project (grant number GDOU2014050203;GDOU2013050314) and Industry-university-research Cooperation Project in Guangdong Province of China (grant number 20138090600155).

语种：英文

外文关键词：DPP-IV inhibitory peptides; Purification; Molecular docking; Antarctic krill; Diabetes mellitus

外文摘要：Dipeptidyl peptidase IV (DPP-IV) played an important role in blood glucose regulation. Inhibition of DPP-IV may improve glycemic control in diabetics by preventing the rapid breakdown of incretin hormones and prolonging their physiological action. In this study, Antarctic krill (Euphausia superba) protein was hydrolyzed using animal proteolytic enzymes. The hydrolysate was purified sequentially by ultrafiltration, gel filtration chromatography and reversed phase high-performance liquid chromatography (RP-HPLC). DPP-IV inhibitory activity of the fractions achieved. from Antarctic krill protein was determined by DPP-IV screening reagent kit. Two purified peptides were identified by Xevo G2-XS QTof mass spectrometer (QTOF-MS). One peptide purified was Ala-Pro (AP) with IC50 values of 0.0530 mg/mL, the other Ile-Pro-Ala (IPA) with IC50 values of 0.0370 mg/mL. They both exhibited strong DPP-IV inhibitory activity. The molecular docking analysis revealed that DPP-IV inhibition by AP and IPA was mainly due to formation of a strong interaction surface force with the 91-96 and 101-105 amino acids of the DPP-IV. Our results suggested that the protein hydrolysate from Antarctic krill can be considered as a promising natural source of DPP-IV inhibitory peptides in the management of diabetes.