Preparation,Identification,and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides
To explore the inhibiting effect of phosvitin phosphopeptide(PPP)on α-amylase,enabling it to regulate blood glucose levels and alleviate type Ⅱ diabetes mellitus.This study employed enzymatic hydrolysis of phosvitin with the inhibition rate of α-amylase as an index,followed by enzyme inhibition kinetics experiments to analyze the inhibitory type of PPP on α-amylase.LC-MS identification was conducted,and molecular docking was performed to screen for highly active α-amylase inhibitory peptides,which were subsequently validated.The results showed that optimal enzymatic hydrolysis conditions involved initial hydrolysis with trypsin(7000 U/g),followed by pepsin(60000 U/g)for 6 h each.The prepared PPP exhibited the highest α-amylase inhibition rate 70.69％±1.71％at a concentration of 7.81×10-3 mg/mL.PPP acted as a mixed-type inhibitor.Two novel highly active α-amylase inhibitory peptides FGTEPDAK and IWGR were identified and screened,exhibiting IC50 values of(0.80±0.14)×10-3 mg/mL and(1.80±0.31)×10-3 mg/mL,respectively.Both extremely significantly lower than the positive control acarbose's IC50 value(3.17±0.47)× 10-3 mg/mL(P＜0.01).This study highlights the potential use of PPP as a new hypoglycemic substance in developing functional foods for alleviating type Ⅱ diabetes mellitus.
万方数据
维普
