The texture of surimi-like gels made from the protein isolate extracted from catfish byproducts has been proven to be brittle and lack elasticity. To address this issue, varying levels of microbial transglutaminase (MTGase) from 0.1 to 0.6 units/g were applied. MTGase had little effect on the color profile of gels. When MTGase at 0.5 units/g was employed, hardness, cohesiveness, springiness, chewiness, resilience, fracturablity, and deformation were increased by 218, 55, 12, 451, 115, 446, and 71%, respectively. A further increase in added MTGase did not lead to any textural improvement. In comparison to the gels made from fillet mince, the gels made from protein isolate were still lower in cohesiveness. Due to the activated endogenous transglutaminase, a setting step enhanced the textural properties of gels made from fillet mince. However, because of the endogenous proteases-induced protein degradation, the setting step led to a texture deterioration of the gels made from protein isolate. Gels made from protein isolate showed 23-55% higher solubility in reducing solution than in non-reducing solution, suggesting the vital role of disulfide bonds in the gelation process. Due to the different protein composition and conformation, fillet mince and protein isolate exhibited distinct rheological properties. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed the highly denatured protein isolate was susceptible to proteolysis and prone to disulfide formation during the gelation process. It also revealed that MTGase had an inhibitory effect on the proteolysis induced by endogenous enzymes. In view of the susceptibility of the protein isolate to proteolysis during gelation, future research should consider including other enzyme inhibitory agents in the presence of MTGase to improve the gel texture.
Keywords: TPA; catfish byproducts; disulfide bonds; electrophoresis; protein isolate; proteolysis; rheological.