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ARS Home » Southeast Area » Stoneville, Mississippi » Warmwater Aquaculture Research Unit » Research » Publications at this Location » Publication #376149

Research Project: Umbrella Project for Food Safety

Location: Warmwater Aquaculture Research Unit

Title: Comparative studies on the yield and characteristics of myofibrillar proteins from catfish heads and frames extracted by two methods for making surimi-like protein gel products

Author
item TAN, YUQING - Mississippi State University
item GAO, HAORAN - Mississippi State University
item CHANG, SAM - Mississippi State University
item Bechtel, Peter
item MAHMOUD, BARAKAT - Mississippi State University

Submitted to: Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 7/25/2018
Publication Date: 1/30/2019
Citation: Tan, Y., Gao, H., Chang, S., Bechtel, P.J., Mahmoud, B. 2019. Comparative studies on the yield and characteristics of myofibrillar proteins from catfish heads and frames extracted by two methods for making surimi-like protein gel products. Food Chemistry. 272:133-140.

Interpretive Summary: Catfish aquaculture in the US southeastern states is the most important aquaculture in the nation. However, huge amount of by-products, representing about 60% of the total whole fish weight, were produced along with catfish fillet production. The by-product has no value and considered as waste. This manuscript studied the possibility of making value-added surimi-like gel products from the proteins extracted from catfish by-products, and investigated the yield of protein extraction under two extraction conditions. More than 30% of the protein could be recovered. We are the first to show the possibility of extracting proteins from catfish by-products to make fish protein gel products.

Technical Abstract: Fish protein isolates (FPI) were recovered from catfish heads and frames by alkaline extraction (AE) and salt extraction (SE) and made into surimi-like gels. Protein patterns and content, moisture, color, and texture of cooked protein gels were compared with commercial products. Molecular mass as determined by sodium-dodecyl-sulfate poly acrylamide gel electrophoresis indicated that the integrity of major myofibrillar proteins was maintained during the extraction process, and the protein patterns were almost the same with that of the commercial surimi products. The yields of AE-FPI (heads: 36%; frames: 55%) were much higher (p'<'0.05) than that of SE-FPI (heads: 9%; frames: 16%). Firmness of cooked protein gels made from heads was similar with that made from frames. Firmness of cooked protein gels made from FPI extracted by the SE method (heads: 0.45'kg/cm2; frames: 0.43'kg/cm2) was significantly lower (p'<'0.05) than that made from FPI extracted by the AE method (heads: 1.96'kg/cm2; frames: 1.85'kg/cm2).