Angiotensin I-converting enzyme inhibitory activity of enzymatic hydrolysates of goat milk protein fractions |
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| Affiliation: | 1. Department of Chemical Engineering, University of Granada, 18071 Granada, Spain;2. Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark;1. Animal Biochemistry Division, National Dairy Research Institute, Karnal 132 001, Haryana State, India;2. Department of Veterinary Biochemistry, Rajiv Gandhi Institute of Veterinary Education and Research, Kurumbapet, Puducherry 605 009, India;1. State Key Laboratory of Dairy Biotechnology, Shanghai Engineering Research Center of Dairy Biotechnology, Dairy Research Institute, Bright Dairy & Food Co Ltd., Shanghai 200436, China;2. State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China;3. Dairy Science Department, Food Science and Nutrition Division, National Research Centre, Dokki 12311, Giza, Egypt;4. International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu 214122, China;1. Laboratório de Bioquímica e Microbiologia Aplicada, Instituto de Ciência e Tecnologia de Alimentos (ICTA), Universidade Federal do Rio Grande do Sul (UFRGS), 91501-970 Porto Alegre, RS, Brazil;1. State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China;2. Dairy Science Department, National Research Centre, Dokki 12311, Giza, Egypt;3. Synergetic Innovation Center for Food Safety and Nutrition, Jiangnan University, Wuxi, Jiangsu 214122, China |
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| Abstract: | Casein and whey protein fractions from goat milk were hydrolysed by subtilisin and trypsin, individually and in combination, to release angiotensin converting enzyme (ACE)-inhibitory peptides. Selected hydrolysates were fractionated by size exclusion chromatography (SEC) and further characterised. The highest ACE-inhibitory activity was obtained from the casein fraction hydrolysed by the combination of enzymes. SEC presented 4 fractions with fraction F2 (<2.3 kDa) containing the highest concentration of peptides and the highest activity. F2 contained a number of peptides not previously identified from caprine caseins but with structural similarity to other ACE-inhibitory peptides. The most active fraction in relation to protein content was F4 with IC50 between 9.3 and 5.1 μg mL−1. This fraction contained a compound tentatively identified as WY, an active dipeptide not previously reported from caseins. The high inhibitory capacity of these fractions points towards the advantage of implementing a membrane process to concentrate the most active peptides. |
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