Angiotensin-I-Converting Enzyme Inhibitory Activity and Antioxidant Properties of Cryptides Derived from Natural Actomyosin of Catla catla Using Papain
2018
Elavarasan, Krishnamoorthy | Shamasundar, Bangalore Aswathnarayan
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.
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