Angiotensin Converting Enzyme Inhibitory and Antioxidant Activities of Enzymatic Hydrolysates of Korean Native Cattle (Hanwoo) Myofibrillar Proteinopen access
- Authors
- Lee, Seung Yun; Hur, Sun Jin
- Issue Date
- Dec-2017
- Publisher
- HINDAWI LTD
- Citation
- BIOMED RESEARCH INTERNATIONAL, v.2017
- Journal Title
- BIOMED RESEARCH INTERNATIONAL
- Volume
- 2017
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/6303
- DOI
- 10.1155/2017/5274637
- ISSN
- 2314-6133
2314-6141
- Abstract
- 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 5-20mg/mL. These results indicate that HMPH can be cheaply produced using Alkaline-AK and applied as a potential ACE inhibitor and antioxidant.
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