Anti‐hypercholesteraemic and antioxidative activities of camel skin gelatin hydrolysate: effect of enzyme type, enzyme: substrate ratio and time of hydrolysis

Abstract

SummaryCamel skin gelatin hydrolysate (CSGH) was prepared using different proteolytic enzymes [alcalase (A), protease (P) and their combination (AP (1:1))], hydrolysis time (2, 4 and 6 h) and enzyme: substrate (E/S) ratio (1%, 3% and 5%). In general, the degree of hydrolysis (DH) increased with increasing hydrolysis time for all enzyme treatments. CSGHs generated with alcalase showed significantly higher lipase (LP) inhibitory activity compared with protease‐derived CSGH at all hydrolysis conditions (P < 0.05). Whereas higher cholesterol esterase (CE) inhibitory activity was observed with CSGH produced by protease (P < 0.05). However, when CSGHs were produced using AP, the highest LP and CE inhibitory activity were recorded at 3 and 1% E/S ratio during 2 and 4 h of hydrolysis, respectively (P < 0.05). Antioxidant assays revealed that CSGHs showed improved radical scavenging activities compared with native CSG (P < 0.05). Overall results indicated that CSGHs with higher in vitro anti‐hypercholesteraemic and antioxidant activities could be obtained by enzymatic hydrolysis.