Characterization of EstDR4, a Novel Cold-Adapted Insecticides-Metabolizing Esterase from Deinococcus radiodurans

Cold-adapted esterases are attracting increasing attention owing to their prospective use in biotechnology. In this study, a novel cold-adapted family esterase EstDR4 was identified and obtained from extremophile Deinococcus radiodurans (D. radiodurans). EstDR4 displayed significant substrate preference towards short and medium chain monoesters (C2-C12). It also showed regioselectivity, enantioselectivity and degradation effects on four insecticides. The optimum temperature and pH for EstDR4 activity were 30 degrees C and pH 8, respectively. Additionally, EstDR4 exhibited relatively high catalytic activity at 0 degrees C and high stability from 10-40 degrees C, with over 80% of its initial activity retained after 1 h of incubation. Moreover, EstDR4 activity was stimulated by Tween 80 and Triton X-100, and inhibited by metal ions such as Co2+, Cu2+ and Zn2+ and several organic solvents. Thus, this enzyme shows development potential for many industrial biotechnological applications, including the manufacture of thermolabile pharmaceutical products, cold-wash detergents and insecticide biodegradation.

Automated summary

A novel cold-adapted family esterase EstDR4 was identified from extremophile Deinococcus radiodurans, showing significant substrate preference towards short and medium chain monoesters and degradation effects on insecticides. EstDR4 displayed high catalytic activity and stability at low temperatures, with optimal activity at 30 degrees C and pH 8. The enzyme's activity was influenced by metal ions and organic solvents, indicating its potential for various biotechnological applications.