Hydrolysis mechanism of carbendazim hydrolase from the strain Microbacterium sp. djl-6F

Ji, Lei; Sang, Wei; Ren, Lijun; Hu, Shibin; Chen, Peng

doi:10.1016/j.jes.2016.05.027

Cited by 23 publications

(14 citation statements)

References 19 publications

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“…The molecular mass of HY-1 was almost 30 kDa, which is identical to the calculation based on hy-1 gene sequence. The molecular mass of HY-1 was similar to the other reported MBC-degradation enzymes, belonging to hydrolase family [8,9] . Then the HY-1 was purified by Ni-NTA agarose gel and the result was displayed in Figure 3c.…”

Section: Cloning Expression and Purification Of Hy-1supporting

confidence: 78%

“…The relative enzymatic activities of E-HY1 cell free extract and purified HY-1 were 0.021 U/mg and 40 U/mg, respectively. The enzymatic activity of HY-1 was slightly higher than the previous reports [9,17] . In total, the hydrolyzing results certified that MBC was degraded by HY-1, and enzymatic assay suggested that HY-1 is a proper protein for restoration of MBC-contaminated soil and food.…”

Section: Metabolite Characterization and Enzyme Assaycontrasting

confidence: 72%

“…MBC hydrolyzing enzyme MheI from Microbacterium sp. had been reported for MBC degradation and several mutations had been researched for higher activity [9] . Nevertheless, the bioremediation on MBC contaminated water and food was not conducted.…”

Section: Introductionmentioning

confidence: 99%

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Identification of a novel hydrolase encoded by hy-1 from Bacillus amyloliquefaciens for bioremediation of carbendazim contaminated soil and food

Liu¹,

Chi²,

Ge³

2019

International Journal of Agricultural and Biological Engineering

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Carbendazim (MBC) is an effective antifungal and antibacterial pesticide in agricultural applications. However, the MBC-contaminated soil and food are difficult to be restored. In this work, a novel MBC-hydrolase HY-1 encoded by gene hy-1 from an isolated MBC-degrading bacteria Bacillus amyloliquefaciens has been screened and identified. The 858 bp hydrolase gene was expressed in E. coli BL21 and the 32 kDa hydrolase HY-1 was purified. The purified HY-1 was able to catalyze MBC into 2-aminobenzimidazole (2-AB) without the need for any cofactors. Then bioremediation experiment was conducted and both the strain Car4 and cell crude extract of E. coli (pET-hy1) accelerated MBC degradation in soil. Moreover, purified HY-1 was available in removing MBC residue on the surface of cucumber. This work explored the possibility of microbial and enzymatic bioremediation on MBC-contaminated soil and food, provide a new way for bioremediation of pesticide contaminations.

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Section: Cloning Expression and Purification Of Hy-1supporting

confidence: 78%

Section: Metabolite Characterization and Enzyme Assaycontrasting

confidence: 72%

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Identification of a novel hydrolase encoded by hy-1 from Bacillus amyloliquefaciens for bioremediation of carbendazim contaminated soil and food

Liu¹,

Chi²,

Ge³

2019

International Journal of Agricultural and Biological Engineering

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“…djl-6F has been purified and characterised. The enzyme does not require any co-factor and has two cysteine residues, Cys16 and Cys222, involved in hydrolysis ( Lei et al, 2017 ). Similarly, the carbendazim hydrolase, MheI from Mycobacterium sp.…”

Section: Bacterial Metabolism Of Carbamate Pesticidesmentioning

confidence: 99%

Conserved Metabolic and Evolutionary Themes in Microbial Degradation of Carbamate Pesticides

2021

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Carbamate pesticides are widely used as insecticides, nematicides, acaricides, herbicides and fungicides in the agriculture, food and public health sector. However, only a minor fraction of the applied quantity reaches the target organisms. The majority of it persists in the environment, impacting the non-target biota, leading to ecological disturbance. The toxicity of these compounds to biota is mediated through cholinergic and non-cholinergic routes, thereby making their clean-up cardinal. Microbes, specifically bacteria, have adapted to the presence of these compounds by evolving degradation pathways and thus play a major role in their removal from the biosphere. Over the past few decades, various genetic, metabolic and biochemical analyses exploring carbamate degradation in bacteria have revealed certain conserved themes in metabolic pathways like the enzymatic hydrolysis of the carbamate ester or amide linkage, funnelling of aryl carbamates into respective dihydroxy aromatic intermediates, C1 metabolism and nitrogen assimilation. Further, genomic and functional analyses have provided insights on mechanisms like horizontal gene transfer and enzyme promiscuity, which drive the evolution of degradation phenotype. Compartmentalisation of metabolic pathway enzymes serves as an additional strategy that further aids in optimising the degradation efficiency. This review highlights and discusses the conclusions drawn from various analyses over the past few decades; and provides a comprehensive view of the environmental fate, toxicity, metabolic routes, related genes and enzymes as well as evolutionary mechanisms associated with the degradation of widely employed carbamate pesticides. Additionally, various strategies like application of consortia for efficient degradation, metabolic engineering and adaptive laboratory evolution, which aid in improvising remediation efficiency and overcoming the challenges associated with in situ bioremediation are discussed.

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“…Microbacterium sp. djl-6F ( Lei et al, 2017 ), Mycobacterium sp. strain djl-10 ( Zhang et al, 2017a ), Pseudomonas sp.…”

Section: Introductionmentioning

confidence: 99%

Construction and Characterization of an Intergeneric Fusant That Degrades the Fungicides Chlorothalonil and Carbendazim

et al. 2022

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Bordetella sp. CTN-16 (GenBank FJ598326) can degrade chlorothalonil (CTN) but not carbendazim (MBC), and Microbacterium sp. MBC-3 (GenBank OK667229) can degrade MBC but not CTN. A functional strain BD2 was obtained by protoplast fusion of CTN-16 and MBC-3 to generate a fusant with improved degradation efficiency of CTN and MBC. Fusant-BD2 with eighth transfer on a medium containing CTN and two antibiotics was obtained. To identify and confirm the genetic relationship between parental strains and fusion strain BD2, scanning electron microscopy (SEM), random amplified polymorphic DNA (RAPD), and 16S ribosomal RNA (rRNA) gene sequences analysis were carried out. SEM analysis illustrated BD2 and its parents had some slight differences in the cell morphology. Fusant-BD2 not only possessed the same bands as parental strains but also had its specific bands analyzed through RAPD. The genetic similarity indices for BD2 and its parental strains CTN-16 and MBC-3 are 0.571 and 0.428, respectively. The degradation rates of CTN and MBC were 79.8% and 65.2% in the inorganic salt solution containing 50 mg·L−1 CTN and 50 mg·L−1 MBC, respectively, and the degradation efficiencies were better than the parental strains CTN-16 and MBC-3. This study provides a prospect for the application of fusion strain BD2 in bioremediation of CTN and MBC contaminated sites.

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Hydrolysis mechanism of carbendazim hydrolase from the strain Microbacterium sp. djl-6F

Cited by 23 publications

References 19 publications

Identification of a novel hydrolase encoded by hy-1 from Bacillus amyloliquefaciens for bioremediation of carbendazim contaminated soil and food

Identification of a novel hydrolase encoded by hy-1 from Bacillus amyloliquefaciens for bioremediation of carbendazim contaminated soil and food

Conserved Metabolic and Evolutionary Themes in Microbial Degradation of Carbamate Pesticides

Construction and Characterization of an Intergeneric Fusant That Degrades the Fungicides Chlorothalonil and Carbendazim

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