Protein extraction pH and cross-linking affect physicochemical and textural properties of protein gels made from channel catfish by-products.

Abstract

Channel catfish farming is very important aquaculture industry in the southern states of the USA. However, huge amounts of by-products are generated from catfish fillet-processing. The by-products (mostly heads and bone frames) are excellent sources of proteins. Currently, catfish by-product has little value, and is regarded as a 'waste', which if not utilized properly could cause serious environmental pollution. Therefore, to find a way to utilize those by-products is critical for the economy of aquaculture. Protein isolates were extracted from the mixture of catfish by-products (heads and frames) under different alkaline conditions (pH 7.5-11) and made into protein gels. Secondary structures of extracted protein isolates were studied. Microbial transglutaminase (MTGase, 0-4 U g-1 proteins) was incorporated to improve gel structure. Gelling, physicochemical, textural and thermal properties of protein gels treated with/without MTGase were investigated. Protein pattern changes of MTGase-treated protein gels were studied and the microstructure of the protein gels was analyzed. Alpha-helicity of protein isolates made at pH 11 was 21.5% lower than that extracted at pH 8.5. Storage modulus (G') of protein gel decreased with increasing extraction pH (pH > 9) of the corresponding protein isolate. MTGase treatment exhibited significant effects on denaturation temperature and enthalpy of protein gels. Excessive MTGase (>2 U g-1 ) could weaken the gel structure. Protein isolates can be extracted from catfish by-products and made into protein gels, which are a value-added product. © 2021 Society of Chemical Industry.