Production of Transglutaminase by Streptoverticillium ladakanum NRRL-3191 Using Glycerol as Carbon Source

The enzyme transglutaminase (TG) catalyses the formation of covalent bonds between adjacent proteins, thereby improving the gel structure of proteins and has important applications for the food industry. The aims of this work were: (i) to elucidate the effect of agitation speed during the biotechnological production of TG by Streptoverticillium ladakanum NRRL-3191 using glycerol as carbon source; and (ii) to improve TG production by optimising the composition of media based on glycerol, xylose and casein. An agitation speed of 250 rpm and a fermentation time of 72 h resulted in the optimal enzymatic activity (0.628 U/mL) with a productivity of 0.087 U/(mL·h). The composition of media with glycerol, xylose and casein were optimised using an experimental design to improve TG production. The model predicts that the maximum TG activity (0.725 U/mL) can be obtained using glycerol 50.5 g/L and casein 20 g/L without the addition of xylose.