Abstract
Transglutaminase (TG, EC 2.3.2.13) is widely used to modify functional properties in food systems, which can catalyze cross-linking reaction of proteins. In this work, microbial transglutaminase (MTG) from Streptomyces netropsis was heterologously expressed in the methylotrophic yeast Komagataella phaffii (Pichia pastoris). The specific activity of recombinant microbial transglutaminase (RMTG) was 26.17 ± 1.26 U/mg, and the optimum pH and temperature were measured as 7.0 and 50°C, respectively. Bovine serum albumin (BSA) was used as a substrate to evaluate the effect of cross-linking reaction, and we found that RMTG had significant (p < 0.05) cross-linking effect for more than 30min reactions. RMTG was further utilized in the investigation of plant-based chicken nuggets. Results showed that the hardness, springiness and chewiness of nuggets increased, and the adhesiveness decreased after RMTG treatment, which can prove that RMTG has the potential to improve the texture properties of plant-based chicken nuggets.
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