Secretion of Bacillus amyloliquefaciens Transglutaminase from Lactococcus lactis and Its Enhancement of Food Gel Properties

(1) Background: Microbial transglutaminases (MTGase) catalyze protein crosslink. This is useful in the food industry to improve gelation, water holding capacity, and emulsifying capacity during foodstuff manufacturing. The production of MTGase in wild-type strains renders low yield and high costs of downstream purification, limiting its industrial applications. (2) Methods: In this work, MTGase from Bacillus amyloliquefaciens BH072 (BaMTGase) has been heterologously expressed in Lactococcus lactis, using the signal peptide Usp45 to direct the secretion of recombinant BaMTGase out of the cell for easier purification. (3) Results: In these conditions, MTGase was purified with a high yield (48.7 +/- 0.2 mg/L) and high enzyme activity (28.6 +/- 0.5 U/mg). Next, BaMTGase was tested for industrial applications. Recombinant BaMTGase and commercial MTGase were used for SPI solution crosslinking. BaMTGase formed a harder gel with higher water-holding capacity and a dense and smooth gel microstructure. (4) Conclusions: This work provides an attractive food-grade cell factory for the food industry and offers a suitable chassis for MTGase production.

Automated summary

This study successfully heterologously expressed BaMTGase in Lactococcus lactis and purified it by directing secretion using a signal peptide. BaMTGase showed superior performance in SPI solution crosslinking, with higher gel strength and water-holding capacity. This work provides an attractive cell factory for the food industry and a suitable platform for MTGase production.