Angiotensin Converting Enzyme Inhibitory and Antioxidant Activities of Enzymatic Hydrolysates of Korean Native Cattle (Hanwoo) Myofibrillar Protein.

The purpose of this study was to determine the angiotensin converting enzyme (ACE) inhibitory and antioxidant activities of myofibrillar protein hydrolysates (HMPHs) of different molecular weights (<3 and <10 kDa) derived from Korean native cattle (Hanwoo breed) using a commercially available and inexpensive enzyme (Alkaline-AK). HMPH of both tested molecular weights had ACE inhibitory activity. Among the antioxidant activities, iron chelation and nitrite scavenging activities were higher in low-molecular-weight peptide of HMPH (<3 kDa), whereas 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity was higher in high-molecular-weight peptide of HMPH (<10 kDa). HMPH did not induce cytotoxicity in RAW 264.7 cells at concentrations of 5-20 mg/mL. These results indicate that HMPH can be cheaply produced using Alkaline-AK and applied as a potential ACE inhibitor and antioxidant.