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Characteristics and functional properties of sarcoplasmic proteins from threadfin bream (Nemipterus hexodon)

Krasaechol, N, Sanguandeekul, R, Duangmal, K and Owusu-Apenten, R (2005) Characteristics and functional properties of sarcoplasmic proteins from threadfin bream (Nemipterus hexodon). In: 2005 IFT Annual Meeting, July 16 - 20; New Orleans, LA, New Oleans. Institute of Food Technologists. 1 pp. [Conference contribution]

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URL: http://ift.confex.com/ift/2005/techprogram/paper_29887.htm

Abstract

Proteins from surimi processing wastewater make up 20-35% of total proteins from fish muscle. Dehydrated fish sarcoplasmic protein (FSP) from surimi wastewater is currently used as feed. The functionality FSP need to examined to allow its use as a valuable food ingredient. The objectives of this study are to investigate the structure and functionality of FSP from threadfin bream used commercially for surimi manufacture in Thailand. Fish fillet was homogenized with (1:5 w/v) Na-phosphate buffer (0.1M, pH 7.0), centrifuged at 4 o C (12,000g - 15 min) and the product freeze-dried for storage. Dissolved FSP was subjected to several analyses: sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), protease activity assay, apparent lysine and total sulfhydryl content. A standardized foaming test was applied to FSP using sodium caseinate and beta-lactoglobulin for comparison. SDS-PAGE showed that FSP isolate contained 4 size ranges of polypeptides: 8 to 10 kDa (5%), 22 to 26 kDa (12%), 47 to 59 kDa (53%) and 109 to 283 kDa (30%). About 56-67% alkaline protease activity from fish homogenate was retained in FSP isolate. The amino and sulfhydryl contents in FSP were 172 (±1.14) m moles/ g and 32.05 (±0.87) m moles/ g, respectively. FSP was soluble at pH 2 to 4 and pH 7 to 9 with minimum solubility at pH 5.0. The foaming capacity of FSP was 62.5 to 65.2% of the values obtained for beta-lactoglobulin and sodium caseinate and was not pH-sensitive at pH 2-pH 9. Anions (sodium, ammonium, magnesium and calcium: 0.2 M) had no effect on the foaming capacity of FSP but foam stability increased in the presence of magnesium. These trends were similar to those obtained for caseinate or beta-lactoglobulin. These interim results show FSP is a potentially useful protein ingredient. Studies of the gelation and emulsifying characteristics of FSP are in progress.

Item Type:Conference contribution (Poster)
Faculties and Schools:Faculty of Life and Health Sciences > School of Biomedical Sciences
Faculty of Life and Health Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute > Nutrition Innovation Centre for Food and Health (NICHE)
Biomedical Sciences Research Institute
ID Code:24457
Deposited By: Dr Richard Owusu-Apenten
Deposited On:09 Jan 2013 11:10
Last Modified:09 Jan 2013 11:10

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