Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinella

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• 作者：Ali Bougatef ; Naima Nedjar-Arroume ; Laï ; la Manni ; Rozenn Ravallec ; Ahmed Barkia ; Didier Guillochon ; Moncef Nasri
• 关键词：Heads and viscera ; Antioxidant activity ; Radical-scavenging activity ; Peptide ; Mass spectrometry ; Sardinella aurita
• 刊名：Food Chemistry
• 出版年：2010
• 出版时间：1 February 2010
• 年：2010
• 卷：118
• 期：3
• 页码：559-565
• 全文大小：323 K

文摘

In order to utilise sardinelle (Sardinella aurita) protein by-products, which is normally discarded as industrial waste in the process of fish manufacturing, heads and viscera proteins were hydrolysed by different proteases to obtain antioxidative peptides. All hydrolysates showed different degrees of hydrolysis and varying degrees of antioxidant activities. Hydrolysate generated with crude enzyme extract from sardine (Sardina pilchardus) displayed high antioxidant activity, and the higher DPPH radical-scavenging activity (87 ± 2.1 % at 2 mg/ml) was obtained with a degree of hydrolysis of 6 % . This hydrolysate was fractionated by size exclusion chromatography on a Sephadex G-25 into eight major fractions (P₁–P₈). Fraction P₄, which exhibited the highest DPPH scavenging activity, was then fractionated by reversed-phase high performance liquid chromatography (RP-HPLC). Seven antioxidant peptides were isolated. The molecular masses and amino acids sequences of the purified peptides were determined using ESI-MS and ESI-MS/MS, respectively. Their structures were identified as Leu-His-Tyr, Leu-Ala-Arg-Leu, Gly-Gly-Glu, Gly-Ala-His, Gly-Ala-Trp-Ala, Pro-His-Tyr-Leu and Gly-Ala-Leu-Ala-Ala-His. The first peptide displayed the highest DPPH radical-scavenging activity (63 ± 1.57 % ; at 150 μg/ml) among these peptides.

The results of this study suggest that sardinelle by-products protein hydrolysates are good source of natural antioxidants.