Transglutaminase (TG) was used to produce films from whey protein isolate, soybean 11S globulin and a mixture of the two (1:1, wt/wt). Solubility of TG cross‐linked films was lower than that of control films at pH 3, 4, 6 and 8. Solubility of control films in 6.6M urea and in 10% SDS was higher than that of TG cross‐linked films. Hydrolysis of control and TG cross‐linked films by trypsin and α‐chymotrypsin was similar after 24h incubation. Mean thickness of films ranged from 69 to 77 μm and there were no differences among thicknesses. Average tensile strength values of TG cross‐linked films were two times greater than those of the homologous controls.
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Yıldırım et al. (1998) studied this question.
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