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Jeewanthi RK, Kim MH, Lee NK, et al. Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes. Korean J Food Sci Anim Resour. 2017;37(1):62-70doi: 10.5851/kosfa.2017.37.1.62.
Jeewanthi, R. K., Kim, M. H., Lee, N. K., Yoon, Y. C., & Paik, H. D. (2017). Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes. Korean journal for food science of animal resources, 37(1), 62-70. https://doi.org/10.5851/kosfa.2017.37.1.62
Jeewanthi, Renda Kankanamge Chaturika, et al. "Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes." Korean journal for food science of animal resources vol. 37,1 (2017): 62-70. doi: https://doi.org/10.5851/kosfa.2017.37.1.62
Jeewanthi RK, Kim MH, Lee NK, Yoon YC, Paik HD. Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes. Korean J Food Sci Anim Resour. 2017;37(1):62-70. doi: 10.5851/kosfa.2017.37.1.62. Epub 2017 Feb 28. PMID: 28316472; PMCID: PMC5355585.
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Korean J Food Sci Anim Resour. 2017;37(1):62-70. doi: 10.5851/kosfa.2017.37.1.62. Epub 2017 Feb 28.

Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes.

Korean journal for food science of animal resources

Renda Kankanamge Chaturika Jeewanthi, Myeong Hee Kim, Na-Kyoung Lee, Yoh Chang Yoon, Hyun-Dong Paik

Affiliations

  1. Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 05029, Korea.
  2. Department of Food Science and Biotechnology of Animal Resources, Konkuk University, Seoul 05029, Korea; Bio/Molecular Informatics Center, Konkuk University, Seoul 05029, Korea.

PMID: 28316472 PMCID: PMC5355585 DOI: 10.5851/kosfa.2017.37.1.62

Abstract

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.

Keywords: bioactive peptides; protease S; proteolytic activity; whey protein hydrolysates

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