Angiotensin-I-Converting Enzyme Inhibitory Activity and Antioxidant Properties of Cryptides Derived from Natural Actomyosin of Catla catla Using Papain

Abstract

Natural actomyosin (NAM) from the freshwater fish Catla catla was extracted and hydrolyzed using papain enzyme at different enzyme-to-substrate ratios (0.5%, 1.0%, 2.0%, 5.0%, and 10%) to obtain the cryptides with different degrees of hydrolysis (DH). Derived cryptides were evaluated for bioactive properties such as angiotensin-I-converting enzyme (ACE) inhibitory activity and antioxidant properties. The pattern of hydrolysis of NAM as a function of time revealed that major protein components such as myosin and actin were hydrolyzed within 10 min of hydrolysis. The cryptides obtained with the DH of 29.4% had significantly higher ACE inhibitory activity and linoleic acid peroxidation inhibitory activity (P<0.05). A higher DPPH free radical-scavenging activity and ferric-reducing power were exhibited by the NAM cryptide mixture obtained with the DH of 17.38 and 26.2%, respectively. The natural actomyosin could be a potential precursor to produce the cryptides with therapeutical and antioxidant properties.