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논문 기본 정보

자료유형
학술저널
저자정보
Jeewanthi, Renda Kankanamge Chaturika (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) Kim, Myeong Hee (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) Lee, Na-Kyoung (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) Yoon, Yoh Chang (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) Paik, Hyun-Dong (Department of Food Science and Biotechnology of Animal Resources, Konkuk University)
저널정보
한국축산식품학회 한국축산식품학회지 한국축산식품학회지 제37권 제1호
발행연도
2017.1
수록면
62 - 70 (9page)

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The aim of this study was identifying a suitable food grade enzymes to hydrolyze whey protein concentrates (WPCs), to give the highest bioactivity. WPCs from ultrafiltration retentate were adjusted to 35% protein (WPC-35) and hydrolyzed by enzymes, alcalase, ${\alpha}-chymotrypsin$, pepsin, protease M, protease S, and trypsin at different hydrolysis times (0, 0.5, 1, 2, 3, 4, and 5 h). These 36 types of hydrolysates were analyzed for their prominent peptides ${\beta}-lactoglobulin$ (${\beta}-Lg$) and ${\alpha}-lactalbumin$ (${\alpha}-La$), to identify the proteolytic activity of each enzyme. Protease S showed the highest proteolytic activity and angiotensin converting enzyme inhibitory activity of IC50, 0.099 mg/mL (91.55%) while trypsin showed the weakest effect. Antihypertensive and antioxidative peptides associated with ${\beta}-Lg$ hydrolysates were identified in WPC-35 hydrolysates (WPH-35) that hydrolyzed by the enzymes, trypsin and protease S. WPH-35 treated with protease S in 0.5 h, responded positively to usage as a bioactive component in different applications of pharmaceutical or related industries.

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