Preparation of angiotensin-I-converting enzyme inhibitory hydrolysates from unsupplemented caprine whey fermentation by various cheese microflora |
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Affiliation: | 1. Department of Biochemistry and Biotechnology, Faculty of Agriculture, Kagoshima University, Kagoshima 890–0065, Japan;2. Department of Food Hygiene and Control, Faculty of Veterinary Medicine, South Valley University, Qena 83523, Egypt;3. Department of Food Hygiene and Control, Faculty of Veterinary Medicine, Assiut University, Assiut 71515, Egypt |
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Abstract: | Unsupplemented caprine whey was fermented by 25 cheese microflora in order to produce peptides from α-lactalbumin (α-la) and/or β-lactoglobulin (β-lg) hydrolysis. Fourteen hydrolysates enriched in peptides mainly released from α-la were obtained. Angiotensin-I-converting enzyme (ACE) inhibitory activity of each hydrolysate was investigated. Six of them had high ACE inhibitory activities ranging from 31% to 56%. The highest ACE inhibitory activity was obtained after whey fermentation by the microflora from 18 months ripened Comté cheese. The microflora was identified as a co-culture of Candida parapsilosis and Lactobacillus paracasei. Hydrolysate activity remained stable after pepsin, trypsin and chymotrypsin treatments simulating an in vitro gastrointestinal digestion. This hydrolysate was further fractionated by RP-HPLC. The peptide exhibiting the highest ACE inhibitory activity was characterised as WLAHK (α-la f(104–108): Trp–Leu–Ala–His–Lys). WLAHK was resistant toward pepsin and trypsin treatments but was digested by chymotrypsin. |
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