Genome mining reveals the genes of carboxypeptidase for OTA-detoxification in Bacillus subtilis CW14

Xu, Xianli; Pang, Min; Liu, Jiawei; Wang, Yuping; Wu, Xiaoyan; KunLun, Huang; Liang, Zhihong

doi:10.1016/j.ijbiomac.2021.07.085

Cited by 32 publications

(15 citation statements)

References 81 publications

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“…In the other study, the dacA and dacB genes responsible for carboxypeptidase production from the B. subtilis CW 14 strain were expressed in E. coli . The purified dacA protein provided 71.3% OTA biodegradation in 24 h (Xu et al, 2021 ). Ochratoxinase (OTase) obtained from A. niger strain W-35 was successfully expressed in E. coli BL21 and degraded OTA at a ratio of 85.1% for 12 h (Zhao et al, 2020 ).…”

Section: Resultsmentioning

confidence: 99%

Ochratoxin A biodegradation by Agaricus campestris and statistical optimization of cultural variables

Söylemez,

Yamaç,

Eninanç

et al. 2023

Food Sci Biotechnol

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The goal of this study is to identify the optimum conditions for ochratoxin A (OTA) biodegradation by the supernatant of Agaricus campestris strain. The Plackett–Burman and Box–Behnken methods were used to determine optimum OTA degradation conditions of Agaricus campestris under various incubation conditions. The Plackett–Burman method was planned through 16 varied experiments with 15 variants. The three most potent variants, sucrose, yeast extract and wheat bran, were selected using the Box–Behnken methodology. Ochratoxin A biodegradation ratio of 46.67% has been specified in only 1 h under ideal growing conditions. This is the first report on the optimization of OTA biodegradation by Agaricus campestris. When compared to previously published articles, it can be asserted that Agaricus campestris has promise based on its OTA biodegradation ratio in only 1 h of reaction time.

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Section: Resultsmentioning

confidence: 99%

Ochratoxin A biodegradation by Agaricus campestris and statistical optimization of cultural variables

Söylemez,

Yamaç,

Eninanç

et al. 2023

Food Sci Biotechnol

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“…neg1 and enzyme PJ_1540 ( 17 ), strain Bacillus amyloliquefaciens ASAG1 and enzyme rCP ( 18 ), strain Lysobacter sp. CW239 and enzyme CP4 ( 9 , 20 ), and Bacillus subtilis CW14 and enzyme DacA ( 19 , 25 ). The degradation characteristics of the strains shown above might share similar degradation modes as strain CW117, which contains multiple genes for joint degradation, but the exact degradation mechanisms in these degradation strains are rarely focused.…”

Section: Discussionmentioning

confidence: 99%

Isoenzyme N -Acyl- l -Amino Acid Amidohydrolase NA Increases Ochratoxin A Degradation Efficacy of Stenotrophomonas sp. CW117 by Enhancing Amidohydrolase ADH3 Stability

et al. 2022

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“…The first reported microbial (fungal) ochratoxinase was an Aspergillus niger amidase (Dobritzsch et al 2014 ). Later, bacterial proteins annotated as putative carboxypeptidases from Bacillus amyloliquefaciens ASAG1 (Chang et al 2015 ), Bacillus subtilis CW14 (Hu et al 2018 ; Xu et al 2021 ), Lysobacter sp. CW239 (Wei et al 2020 ), and Acinetobacter sp.…”

Section: Introductionmentioning

confidence: 99%

A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A

Sánchez-Arroyo,

Plaza-Vinuesa,

Abeijón-Mukdsi

et al. 2024

Appl Microbiol Biotechnol

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The presence of ochratoxin A (OTA) in food and feed represents a serious concern since it raises severe health implications. Bacterial strains of the Acinetobacter genus hydrolyse the amide bond of OTA yielding non-toxic OTα and L-β-phenylalanine; in particular, the carboxypeptidase PJ15_1540 from Acinetobacter sp. neg1 has been identified as an OTA-degrading enzyme. Here, we describe the ability to transform OTA of cell-free protein extracts from Acinetobacter tandoii DSM 14970 T, a strain isolated from sludge plants, and also report on the finding of a new and promiscuous α/β hydrolase (ABH), with close homologs highly distributed within the Acinetobacter genus. ABH from A. tandoii (AtABH) exhibited amidase activity against OTA and OTB mycotoxins, as well as against several carboxypeptidase substrates. The predicted structure of AtABH reveals an α/β hydrolase core composed of a parallel, six-stranded β-sheet, with a large cap domain similar to the marine esterase EprEst. Further biochemical analyses of AtABH reveal that it is an efficient esterase with a similar specificity profile as EprEst. Molecular docking studies rendered a consistent OTA-binding mode. We proposed a potential procedure for preparing new OTA-degrading enzymes starting from promiscuous α/β hydrolases based on our results. Key points • AtABH is a promiscuous αβ hydrolase with both esterase and amidohydrolase activities • AtABH hydrolyses the amide bond of ochratoxin A rendering nontoxic OTα • Promiscuous αβ hydrolases are a possible source of new OTA-degrading enzymes

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Genome mining reveals the genes of carboxypeptidase for OTA-detoxification in Bacillus subtilis CW14

Cited by 32 publications

References 81 publications

Ochratoxin A biodegradation by Agaricus campestris and statistical optimization of cultural variables

Ochratoxin A biodegradation by Agaricus campestris and statistical optimization of cultural variables

Isoenzyme N -Acyl- l -Amino Acid Amidohydrolase NA Increases Ochratoxin A Degradation Efficacy of Stenotrophomonas sp. CW117 by Enhancing Amidohydrolase ADH3 Stability

A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A

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