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The Evaluation of Dipeptidyl Peptidase (DPP)-IV, α-Glucosidase and Angiotensin Converting Enzyme (ACE) Inhibitory Activities of Whey Proteins Hydrolyzed with Serine Protease Isolated from Asian Pumpkin (Cucurbita ficifolia)

2014/05/31 by Konrad Babij, Dąbrowska Anna, Marek Szołtysik +3 · 1 citation
Biochemistry, Genetics and Molecular Biology · Medicine · Nursing · #Protein Hydrolysis and Bioactive Peptides #Biochemical effects in animals #Infant Nutrition and Health

paper · pdf · doi:10.1007/s10989-014-9413-0

openalex publication_date 2014/05/31 · openalex created_date 2016/06/24 · openalex updated_date 2026/07/23

Abstract

). Hydrolysates were further fractionated by ultrafiltration using membranes with cut-offs equal 3 and 10 kDa. Peptide fractions of molecular weight lower than 3 and 3-10 kDa were further subjected to the RP-HPLC. Separated preparations were investigated for their potential as the natural inhibitors of dipeptidyl peptidase (DPP-IV), α-glucosidase and angiotensin converting enzyme (ACE). WPC-80 hydrolysate showed higher inhibitory activities against the three tested enzymes than β-lactoglobulin hydrolysate. Especially high biological activities were exhibited by peptide fractions of molecular weight lower than 3 kDa, with ACE IC50 <0.64 mg/mL and DPP-IV IC50 <0.55 mg/mL. This study suggests that peptides generated from whey proteins may support postprandial glycemia regulation and blood pressure maintenance, and could be used as functional food ingredients in the diet of patients with type 2 diabetes.

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