Biochemical characterization of a tyrosinase from Bacillus aryabhattai and its application

Although lots of tyrosinases have been isolated from bacteria, few studies are focused on tyrosinases from Bacillus sp.. In this study, a tyrosinase from B. aryabhattai TCCC 111983 (TYR) was functionally expressed, purified, and then biochemically characterized. The recombinant tyrosinase (rTYR) presented a good catalytic activity in a broad temperature and pH range, retaining over 60% of the relative activity at 30 degrees C-90 degrees C and 45% at pH 3.0 to 10.0. Especially, rTYR exhibited 20% of its maximum activity at 0 degrees C, and it also showed a variable stability towards different effectors. It presented high tolerance towards salinity and chloride, retaining 81% of its original activity in 2 M NaCl. Kinetic parameters indicated that rTYR displayed a relatively good affinity for both L-tyrosine and L-DOPA. Additionally, rTYR demonstrated remarkable advantages on efficient decolorizing azo and anthraquinonic food dyes (carmine and erythrosin), and more five industrial dyes with or without mediators in acidic, neutral, and alkaline conditions. As the first report on the tyrosinase from B. aryabhattai, the aforementioned results indicated that rTYR would be potential for food industrial applications. (c) 2021 Elsevier B.V. All rights reserved.

Automated summary

In this study, a tyrosinase from Bacillus aryabhattai was functionally expressed and characterized. The recombinant enzyme showed good catalytic activity over a wide range of temperatures and pH levels, and also exhibited high tolerance to salinity and chloride. Additionally, it demonstrated efficient decolorization of various industrial dyes under different conditions, indicating its potential for food industrial applications.