Angiotensin I-converting enzyme inhibitory properties of lentil protein hydrolysates: Determination of the kinetics of inhibition

作者：Barbana Chockry; Boye Joyce Irene^*

来源：Food Chemistry, 2011, 127(1): 94-101.

DOI：10.1016/j.foodchem.2010.12.093

• ACE inhibitory activity
• Bioactivity
• Lentil protein hydrolysates
• Lineweaver-Burk

ACE inhibitory activity was studied for different hydrolysates obtained from protein concentrates of two lentil varieties by in vitro gastrointestinal simulation, Alcalase/Flavourzyme, papain and bromelain. Protein/peptide profiles studied by electrophoresis and HPLC-SEC showed a rich composition of the hydrolysates in small peptides ranging in size from 0.244 to 1.06 kDa. ACE inhibitory activity was measured using the HPLC Hippuryl-His-Leu (HHL) substrate method. Significantly different (P < 0.05) IC50 values ranging between 0.053 and 0.190 mg/ml were obtained for different hydrolysates. Furthermore, the inhibition mechanism investigated using Lineweaver-Burk plots revealed a non-competitive inhibition of ACE with inhibitor constants (K-i) between 0.16 and 0.46 mg/ml. These results demonstrate that hydrolysates of lentil proteins obtained by different enzymatic digestions may contain bioactive components.

• 出版日期2011-7-1