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

Jin Wang,Wei Lu,Ming Chen,Yage Zhang,Min Lin,Zhu Liu,Wei Zhang,Zhengfu Zhou

doi:10.3390/app11041864

Abstract

Cold-adapted esterases are attracting increasing attention owing to their prospective use in biotechnology. In this study, a novel cold-adapted family Ⅳ 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 °C and pH 8, respectively. Additionally, EstDR4 exhibited relatively high catalytic activity at 0 °C and high stability from 10–40 °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.

Highlights

Extremophiles as valuable sources of novel enzymes required in industrial applications
As a polyexas valuable sources of novel enzymes required in industrial applications [9]
Extremophiles that thrive in extreme adverse environmental conditions are regarded as valuable sources of novel enzymes required in industrial applications [9]

Summary

Introduction

Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. As an important group of the most utilitarian biocatalysts, lipolytic enzymes, with their ability to catalyze the cleavage and synthesis of ester bonds, have been widely used in many applications including pharmaceuticals, paper, biofuels, and detergent manufacturing [1]. The two main categories of lipolytic enzymes, esterases and lipases, are differentiated by their substrate preference. Esterases prefer hydrolyzing small esters with short fatty acid side chains (≤C10), lipase prefers long fatty acid chains triglycerides (>C10)

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