Camel whey protein hydrolysates displayed enhanced cholesteryl esterase and lipase inhibitory, anti-hypertensive and anti-haemolytic properties

Abstract

Camel whey protein hydrolysates were generated using gastric (pepsin) and pancreatic (trypsin and chymotrypsin) enzymes for 3 and 6 h of hydrolysis time. Hydrolysates were characterized using degree of hydrolysis (DH) and reverse phase-high performance liquid chromatography (RP-HPLC). Camel whey protein hydrolysates (CWPHs) showed DH ranging from 11 to 47.5%, with chymotrypsin (6 h) and trypsin (3 h) generated hydrolysates exhibiting highest and lowest DH, respectively. HPLC analysis revealed that α-lactalbumin underwent complete degradation and newer shorter peptides were generated. Inhibition of cholesteryl esterase, (CE) pancreatic lipase and anti-hypertensive properties via angiotensin converting enzyme (ACE) inhibition were found to be higher in pepsin (6 h) and (3 h) generated CWPHs, respectively. Pepsin (P3 and P6) and trypsin (T6) generated hydrolysates exhibited highest anti-haemolytic activity followed by chymotrypsin generated CWPHs. Whereas, trypsin (T3) generated hydrolysate showed minimum anti-haemolytic activity (8.02% ± 1.40). Overall, CWPHs displayed enhanced inhibition of CE, lipase, ACE and anti-hemolytic properties upon hydrolysis, providing a strong scientific base for their potential to be considered as functional and nutraceutical ingredients. This study provides a strong indication of biologically active peptides responsible for health related bioactive properties reported herein. Future work must include identification of the peptides in the most potent camel whey protein hydrolysates.