Angiotensin I-converting enzyme (ACE) inhibitory activities of sardinelle (Sardinella aurita) by-products protein hydrolysates obtained by treatment with microbial and visceral fish serine proteases
作者： Ali Bougatef , Naima Nedjar-Arroume , Rozenn Ravallec-Plé , Yves Leroy , Didier Guillochon
DOI: 10.1016/J.FOODCHEM.2008.03.074
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摘要: Abstract The angiotensin I-converting enzyme (ACE) inhibitory activities of protein hydrolysates prepared from heads and viscera sardinelle (Sardinella aurita) by treatment with various proteases were investigated. Protein obtained Alcalase®, chymotrypsin, crude preparations Bacillus licheniformis NH1 Aspergillus clavatus ES1, extract sardine (Sardina pilchardus) viscera. All exhibited activity towards ACE. alkaline protease the produced hydrolysate highest ACE (63.2 ± 1.5% at 2 mg/ml). Further, degrees hydrolysis increased increasing proteolysis time. generated was then fractionated size exclusion chromatography on a Sephadex G-25 into eight major fractions (P1–P8). Biological functions all assayed, P4 found to display high activity. IC50 values for by-products fraction 1.2 ± 0.09 0.81 ± 0.013 mg/ml, respectively. showed resistance in vitro digestion gastrointestinal proteases. amino acid analysis GC/MS that rich phenylalanine, arginine, glycine, leucine, methionine, histidine tyrosine. added-value may be improved enzymatic visceral serine sardine.
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