Jeewanthi Renda Kankanamge Chaturika, Kim Myeong Hee, Lee Na-Kyoung, Yoon Yoh Chang, Paik Hyun-Dong
Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 05029, Korea.
Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 05029, Korea; Bio/Molecular Informatics Center, Konkuk University, Seoul 05029, Korea.
Korean J Food Sci Anim Resour. 2017;37(1):62-70. doi: 10.5851/kosfa.2017.37.1.62. Epub 2017 Feb 28.
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, α-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 β-lactoglobulin (β-Lg) and α-lactalbumin (α-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 β-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.
本研究的目的是确定一种合适的食品级酶来水解乳清蛋白浓缩物（WPC），以获得最高的生物活性。将来自超滤截留物的WPC调整至35%蛋白质（WPC-35），并在不同水解时间（0、0.5、1、2、3、4和5小时）用碱性蛋白酶、α-胰凝乳蛋白酶、胃蛋白酶、蛋白酶M、蛋白酶S和胰蛋白酶进行水解。分析这36种水解产物中突出的肽β-乳球蛋白（β-Lg）和α-乳白蛋白（α-La），以确定每种酶的蛋白水解活性。蛋白酶S表现出最高的蛋白水解活性和血管紧张素转换酶抑制活性，IC50为0.099 mg/mL（91.55%），而胰蛋白酶的作用最弱。在经胰蛋白酶和蛋白酶S水解的WPC-35水解产物（WPH-35）中鉴定出与β-Lg水解产物相关的降压和抗氧化肽。用蛋白酶S处理0.5小时的WPH-35在制药或相关行业的不同应用中作为生物活性成分使用时反应良好。
