Enzymatic characterization of transglutaminase from Streptomyces mobaraensis DSM 40587 in high salt and effect of enzymatic cross-linking of yak milk proteins on functional properties of stirred yogurt

Streptomyces transglutaminase (TGase) purified from high-salt medium was characterized and applied into yak yogurts. The purified enzyme presented a Michaelis constant of 40.47 mmol and a maximum velocity of 44.44 U/mg of protein for N-carboxybenzoyl-L-glutaminyl-glycine in the hydroxamate procedure. The purified TGase exhibited optimum activity at 55 degrees C and pH 6.0. The enzyme was not stable above 50 degrees C and was stable within a pH range of 5.0 to 10.0 at 4 degrees C for 12 h and pH 5.0 to 9.0 at 37 degrees C for 30 min. The TGase activity was riot affected by Ca2+, K+, Ba2+, or Na+, but slightly inhibited by Fe2+, Mg2+, and Mn2+, and strongly by Cu2+ and Zn2+. To explore yak milk products, it was used to produce yogurt and TGase was used. It was found that TGase-catalyzed cross-linking was effective in improving functional properties of stirred yak yogurt. Treated yogurt produced a strong acid gel, higher consistency, cohesiveness, index of viscosity, and creamier mouth feel than the untreated product. Furthermore, yak yogurt treated with TGase presented lower wet yak hair or sweat odor, or both. Therefore, TGase can be used to pave the way for exploration of novel yak products to overcome the issues of peculiar wet yak hair or sweat odor, or both.