Abstract
In order to determine the maximum activity range of transglutaminase (TG) in ice cream, the central composite design was used and the TG concentration along with the reaction time and temperature were evaluated. The rheological behavior of the ice cream mix that provided the best response and the determination of the protein cross-linking by electrophoresis (SDS-PAGE) were evaluated. It was observed that the TG increased the consistency index and favored the pseudoplastic behavior of the ice cream samples. The maximum response (0.69 Pa s n) was obtained using a TG concentration of 4 U g −1 protein at 56.8 °C with a reaction time of 90 min. The protein cross-linking was confirmed by electrophoresis, which showed that κ-casein was more susceptible to attack from TG than whey proteins.
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