Enhancement of the Thermostability of Transglutaminase from Streptomyces hygroscopicus by Engineering a Disulfide Bond

Abstract:

In this study, transglutaminase (MTG) from S. hygroscopicus was molecularly modified to improve the thermostability. Mutant MTG (4-284) containing a disulfide bond in the N-terminal region was constructed through sequence aligment, structure analysis and the software Disulfide by Design. After treatment at 55 ℃ for 10 min, MTG (4-284) remained 95% activity whereas MTG only retained 15% activity. The T50 values of MTG and MTG (4-284) were 58 and 65 ℃, respectively. Results in this study could improve genetic reconstruction and promote the industry application of MTG.