Inhibitory properties of camel whey protein hydrolysates toward liver cancer cells， dipeptidyl peptidase-IV， and inflammation.

This report describes an investigation of camel whey protein hydrolysates (CWPH) produced by gastric and pancreatic enzymes for their in vitro antidiabetic， anticancer， and anti-inflammatory properties. Degree of hydrolysis (DH) ranged from 8.54 to 47.53%， with hydrolysates generated using chymotrypsin for 6 h displaying the highest DH. Reverse phase-HPLC analysis showed that α-lactalbumin underwent complete degradation， with no intact α-lactalbumin detected in CWPH. The CWPH displayed enhanced antidiabetic activity compared with intact whey proteins; with pepsin- and chymotrypsin-generated CWPH displaying greater inhibition of dipeptidyl peptidase IV (DPP-IV)， α-glucosidase， and α-amylase compared with trypsin-generated CWPH. The highest antiproliferative effect was observed for CWPH generated by chymotrypsin for 3 h， with only 4.5 to 6.5% viable liver cancer cells (HepG2) remaining when tested at concentrations from 400 to 1，000 µg/mL. The highest anti-inflammatory activity was manifested by CWPH generated by pepsin at 6-h hydrolysis. We report enhanced antiproliferative， antidiabetic， and anti-inflammatory activities upon hydrolysis of camel whey proteins， indicating their potential utilization as bioactive and functional ingredients.