Engineering a novel carbaryl-degrading esterase from Bacillus velezensis for enhanced degradability via semi-rational design and whole-cell biocatalysis.

Jiaoqing Li, Guohao Huang, Jie Zeng, Xiaodong Wang, Tan Wang, Lin Li

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Article in World journal of microbiology & biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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6 authors.

Jiaoqing Li *Guangdong Provincial Key Laboratory of Conservation and Precision Utilization of Characteristic Agricultural Resources in Mountainous Areas, School of Life Sciences, Jiaying University, Meizhou, 514015, China.

Guohao Huang *National Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, China.

Jie ZengNational Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, China.

Xiaodong WangNational Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, China.

Tan WangNational Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, China.

Lin LiNational Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, China. lilin@mail.hzau.edu.cn.

Funding

Meizhou City's 2021 Guangdong Provincial Rural Revitalization Strategy Special Fund 2021A0305002National Natural Science Foundation of China 32170124;31770108

6 · The paper itself

Abstract

The carbamate pesticide carbaryl poses significant ecological and health risks due to its widespread misuse and improper long-term disposal. In this study, we engineered a novel bacterial carbaryl-degrading esterase to enhance enzymatic activity, thermostability, and carbaryl degradation through semi-rational design and whole-cell biocatalysis strategies. An esterase, designated Est03320, was identified from Bacillus velezensis MB01B. Phylogenetic analysis revealed it resides in a distinct clade. However, it contains a catalytic domain similar to those of the well-characterized carbaryl-hydrolyzing esterase CarH and the chlorpyrifos-degrading esterase MPH. Est03320 was expressed and purified from Escherichia coli BL21(DE3) cells, demonstrating high hydrolytic activity against short-chain p-nitrophenyl esters and carbaryl. The enzyme exhibits an optimum pH of 6.5 and an optimal temperature of 25 °C, with a K

Indexed as

BacillusCarbarylEsterasesBacterial ProteinsBiocatalysisBiodegradation, EnvironmentalCatalytic DomainEnzyme StabilityEscherichia coliHydrogen-Ion ConcentrationHydrolysisKineticsMutagenesis, Site-DirectedPhylogenyProtein EngineeringRecombinant ProteinsBacterial ProteinsCarbarylEsterasesRecombinant ProteinsBacillus velezensis MB01BCarbarylDegradationEsteraseSemi-rational designThermostabilityWhole-cell biocatalysis

Identifiers

PMID41128773

DOI10.1007/s11274-025-04636-9

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