Comments on the ochratoxin A degradation mechanism by Lysobacter sp. CW239 — Wei Wei et al. (2020)

Yan, Qiushi; Zhang, Xuanjun; Fei, Qingru; Zhou, Yu

doi:10.1016/j.envpol.2021.117063

Cited by 6 publications

(5 citation statements)

References 10 publications

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“…Conversely, the presence of OTA-degrading activity in a cp4 carboxypeptidase knock-out Lysobacter sp. CW239 strain (Qian et al 2021) as well as in an amidohydrolase NA deficient Stenotrophomonas sp. CW117 strain (Chen et al 2022) suggests that some strains could contain multiple enzymes for OTA degradation.…”

Section: Discussionmentioning

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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Section: Discussionmentioning

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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“…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%

“…Growth curves of CW117 and mutants were determined by fresh bacterial culture according to the method of Qian et al ( 20 ). For ROS evaluation, fresh culture of wild-type CW117, the Δna mutant, or the Δ na-adh3 double mutant was inoculated to nutrient broth with different OTA contents (50 and 500 μg/L), and the cultures were collected at 6th and 12th hours for ROS determination.…”

Section: Methodsmentioning

confidence: 99%

“…The studies on OTA degradation by Lysobacter sp. CW239 found that strain CW239 degrades OTA by joint action of multiple detoxifying enzymes, and the identified carboxypeptidase CP4 showed only limited contribution to OTA degradation in the strain; unfortunately, efficient detoxifying enzymes (or genes) remained unknown ( 9 , 20 ). Other than Lysobacter sp.…”

Section: Introductionmentioning

confidence: 99%

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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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“…As previously documented, phylum Actinobacteria contain many highly efficient SA‐degrading bacteria (Chen & Xie, 2018), and family Micromonosporaceae might have the potential to degrade SMX under anaerobic conditions. Besides, Lysobacter is a popular aerobic functional genus that can utilize several organic pollutants (Maeda et al ., 2009; Qian et al ., 2021), and it is also able to metabolize 2,4,6‐trinitrotoluene under anaerobic conditions based on SIP analysis (Gallagher et al ., 2010). Moreover, Lysobacter and family Burkholderiaceae were suggested as the hosts of ARG including SA resistance genes (Cao et al ., 2021; Chen et al ., 2019a), and thus took advantage over other microbes in heavily antibiotic‐contaminated environments and played important roles in in situ anaerobic SMX removal in aquaculture and livestock farming wastewaters‐contaminated wetland sediments.…”

Section: Discussionmentioning

confidence: 99%

Anaerobic sulfamethoxazole‐degrading bacterial consortia in antibiotic‐contaminated wetland sediments identified by DNA‐stable isotope probing and metagenomics analysis

Chen

Yang

et al. 2022

Environmental Microbiology

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Summary Anaerobic degradation has been demonstrated as an important pathway for the removal of sulfonamide (SA) in contaminated environments, and identifying the microorganisms responsible for the degradation of SA is a key step in developing bioaugmentation approaches. In this study, we investigated the anaerobic degradation activity of three SA [sulfadiazine (SDZ), sulfamethazine (SMZ) and sulfamethoxazole (SMX)] and the associated bacterial community in wetland sediments contaminated by aquaculture (in Fujian Province, coded with FJ), livestock farming (in Sichuan Province, coded with SC), or rural wastewaters (in Guangdong Province, coded with GD). Additionally, the combination of DNA‐stable isotope probing (SIP) with metagenomics was further applied to assess the active SA‐degrading microbes using SMX as a model SA. Among SDZ, SMZ and SMX, only SMX could be effectively dissipated, and the degradation of SMX was relatively fast in the microcosms of sediments with higher levels of SA contamination (FJ and SC). The anaerobic biotransformation pathway of SMX was initiated by hydrogenation with the cleavage of the N–O bond on the isoxazole ring. DNA‐SIP revealed that the in situ active anaerobic SMX‐degraders (5, 18 and 3 genera in sediments FJ, SC and GD respectively) were dominated by Proteobacteria in sediments FJ and SC, but by Firmicutes (two Family XVIII members) in sediment GD. Mycobacterium, unclassified Burkholderiaceae and Rhodocyclaceae were identified as the dominant active SMX‐degrading bacteria in both sediments FJ and SC. Higher proportions of antibiotic resistance gene and genes involved in various functional categories were observed in sediments FJ and SC.

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Comments on the ochratoxin A degradation mechanism by Lysobacter sp. CW239 — Wei Wei et al. (2020)

Cited by 6 publications

References 10 publications

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

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

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

Anaerobic sulfamethoxazole‐degrading bacterial consortia in antibiotic‐contaminated wetland sediments identified by DNA‐stable isotope probing and metagenomics analysis

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