Evaluation of antioxidant activity of muscle and skin protein hydrolysates from giant kingfish, Caranx ignobilis (Forsskål, 1775)

Summary To assess the antioxidant properties of fish protein hydrolysate from giant kingfish Caranx ignobilis (Forsskål, 1775), muscle and skin were obtained using various proteases (papain, pepsin, trypsin and α‐chymotrypsin), respectively. Antioxidant activities of the resulting hydrolysates were...

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Bibliographic Details
Published in:International journal of food science & technology Vol. 47; no. 2; pp. 274 - 281
Main Authors: Nazeer, R. A., Anila Kulandai, K.
Format: Journal Article
Language:English
Published: Oxford, UK Blackwell Publishing Ltd 01-02-2012
Wiley-Blackwell
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Summary:Summary To assess the antioxidant properties of fish protein hydrolysate from giant kingfish Caranx ignobilis (Forsskål, 1775), muscle and skin were obtained using various proteases (papain, pepsin, trypsin and α‐chymotrypsin), respectively. Antioxidant activities of the resulting hydrolysates were evaluated using 2, 2‐diphenyl‐1‐picrylhydrazyl radical scavenging activity, reducing power and metal chelating activity. Among the hydrolysates, peptic of muscle (37 ± 1.0; 0.290 ± 0.012; 63.30 ± 0.57) and tryptic of skin (36.2 ± 1.0; 0.190 ± 0.110; 63 ± 0.57) hydrolysates, which had the highest free radical scavenging activity, was subjected to purification using Sephadex G‐25. The fractionated hydrolysates were superior to the original hydrolysates in the antioxidative activity tested. The active fractions (MF2 and SF2) effectively inhibited lipid peroxidation in linoleic acid emulsion system, and the activity was compared with α‐tocopherol. The amino acid profile of MF2 and SF2 showed a high level of essential amino acids, and the most abundant amino acids were in the order His (12.01% and 7.08%), Phe (7.05% and 6.18%) and Lys (6.76% and 4.74%). Conclusively, C. ignobilis muscle and skin hydrolysates could be a promising rich source of natural antioxidants.
Bibliography:ArticleID:IJFS2836
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ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0950-5423
1365-2621
DOI:10.1111/j.1365-2621.2011.02836.x