Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes.
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.
Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 05029, Korea.
Renda Kankanamge Chaturika
RK
Jeewanthi
Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 05029, Korea.
Myeong Hee
MH
Kim
Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 05029, Korea.
Na-Kyoung
NK
Lee
Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 05029, Korea.
Yoh Chang
YC
Yoon
Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 05029, Korea; Bio/Molecular Informatics Center, Konkuk University, Seoul 05029, Korea.
Hyun-Dong
HD
Paik
bioactive peptides; protease S; proteolytic activity; whey protein hydrolysates