Camel whey protein with enhanced antioxidative and antimicrobial properties upon simulated gastro-intestinal digestion.

Background: Whey proteins and their peptide derivatives have attracted a great attention of researchers in the pharmaceutical and nutritional fields, due to their numerous bio-functionalities. Aim: In the present research study, enzymatic protein hydrolysates (CWPHs) from camel whey proteins (CWPs) were produced and investigated for their antioxidant and antimicrobial potentials. Methods: Herein, Pepsin (gastric), and Trypsin and Chymotrypsin (pancreatic) enzymes were used to produce CWPHs. The obtained hydrolysates were characterize to ascertain the level of protein degradation and studies on their antimicrobial and antioxidant potential were conducted. Results: Among all CWPHs, a complete degradation of all different protein bands was perceived with Chymotrypsin-derived CWPHs, whereas, light bands of serum albumin and α-lactalbumin were observed with Trypsin and Pepsin-derived CWPHs. After enzymatic degradation, both CWPHs antioxidant and antimicrobial activities were improved. Chymotrypsin-derived CWPHs demonstrated higher DPPH and ABTS radical scavenging activities, anent the increase in proteolysis time. Compared to unhydrolyzed CWPs, higher metal chelating activities were displayed by Trypsin-derived CWPHs. No significant increase in the FRAP activities was noticed after CWPs hydrolysis using Trypsin and Chymotrypsin, while Pepsin-derived CWPHs showed higher reducing power. In terms of antimicrobial activity, significantly higher bacterial growth inhibition rates were exhibited by CWPHs compared to the unhydrolyzed CWP. Conclusion: Overall, CWPHs displayed enhanced antioxidative and antimicrobial properties.

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.