To develop functional food material with angiotensin converting enzyme (ACE) inhibitory peptides, muscle protein of anchovy, Engraulis japonica was hydrolyzed during 48 hrs by digestive proteases such as pepsin, trypsin, α-chymotrypsin, and commercia...
To develop functional food material with angiotensin converting enzyme (ACE) inhibitory peptides, muscle protein of anchovy, Engraulis japonica was hydrolyzed during 48 hrs by digestive proteases such as pepsin, trypsin, α-chymotrypsin, and commercial proteases such as papain, bromelain, complex enzyme, Flavourzyme, Novozym, Neutrase, Protamex and Alcalase. The only 50% ethanol soluble hydrolysates were tested for inhibitory activity against ACE and yield of 50% ethanol soluble peptide-nitrogen (ESPN_(50)). ACE inhibition effects and yield of ESPN_(50) occurred as hydrolysis time increased to 8 hrs. Among those proteases tested, hydrolysates by Alcalase and α-chymotrypsin had greater ACE inhibitory activity (80 and 74%, respectively) with elevated levels of ESPN_(50) (48 and 58 ㎎/㎖, respectively), while Protamex hydrolysates had greater ACE inhibitory activities (73%) with reduced levels of ESPN_(50) (7.2 ㎎/㎖) than others. Amino acid compositions of 50% ethanol solubles obtained from those hydrolysates were rich in glutamic acid, aspartic acid, cysteine and leucine.