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      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.

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          Abstract

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

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          Author and article information

          Journal
          Food Chem
          Food chemistry
          0308-8146
          0308-8146
          Nov 15 2008
          : 111
          : 2
          Affiliations
          [1 ] Laboratoire de Génie Enzymatique et de Microbiologie - Ecole Nationale d'Ingénieurs de Sfax, B.P "W" 3038 Sfax, Tunisia.
          [2 ] Laboratoire de Procédés Biologiques, Génie Enzymatique et Microbien, IUT A Lille I, BP 179, 59653 Villeneuve d'Ascq Cedex, France.
          [3 ] CNRS Unité Mixte de Recherche 8576, Laboratoire de Glycobiologie Structurale et Fonctionnelle, Université des Sciences et Technologies de Lille, Bâtiment C9, 59655 Villeneuve d'Ascq Cedex, France.
          [4 ] Laboratoire de Génie Enzymatique et de Microbiologie - Ecole Nationale d'Ingénieurs de Sfax, B.P "W" 3038 Sfax, Tunisia. Electronic address: mon_nasri@yahoo.fr.
          Article
          S0308-8146(08)00408-1
          10.1016/j.foodchem.2008.03.074
          26047434
          019abf95-47eb-4833-b9d8-afa657462096
          Copyright © 2008 Elsevier Ltd. All rights reserved.
          History

          ACE inhibitory activities,Enzymatic treatment,Protein hydrolysates,Sardine serine proteases,Sardinelle by-products

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