Cohn's fraction I-S from porcine plasma showed the highest transglutaminase activity, compared to fractions I. 11+III, IV, IV-l. The optimum temperature for incorporating monodancylcadaverine into dimethylated casein was 45C. Plasma transglutaminase in fraction I-S was activated by calcium chloride but was inhibited by N-ethylmaleimide, ethylenediaminetetraacetic acid, and ammonium chloride. The addition of fraction I-S into bigeye snapper surimi resulted in a substantial increase in gel breaking force and deformation, particularly in the presence of calcium chloride and thrombin. No changes in whiteness and water holding capacity were observed in surimi gel with the addition of 0–0.5% of fraction I-S. Fraction I-S was found to catalyze nondisulfide covalent cross-linking of myosin heavy chain. The combination of endogenous and plasma transglutaminase enhanced surimi gelation.
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Benjakul et al. (2001) studied this question.
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