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

Chen, Nan; Fei, Qingru; Luo, Han; Fang, Zemin; Xiao, Yazhong; Du, Zhengjun; Zhou, Yu

doi:10.1128/spectrum.02205-22

Cited by 13 publications

(7 citation statements)

References 37 publications

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“…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. In agreement with this idea, proteins possessing amidohydrolase (Chen et al 2022;Dobritzsch et al 2014;Luo et al 2022;Zhang et al 2019) or carboxypeptidase activity (Chang et al 2015;Hu et al 2018;Liuzzi et al 2017;Wei et al 2020;Xu et al 2022) have been described elsewhere to be able to hydrolyse the amide bond present in the OTA molecule.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, bacterial enzymes able to efficiently transform OTA have been identified in Alcaligenes faecalis DSM 16503 (Zhang et al 2019), and Stenotrophomonas sp. CW117 (Chen et al 2022;Luo et al 2022). In this regard, we have recently reported that the salicylate 1,2-dioxygenase from Pseudaminobacter salicylatoxidans inactivates OTA acting as an amidohydrolase and proposed that metallocarboxypeptidases may be a rich source of potential OTA-degrading enzymes (Sánchez-Arroyo et al 2023).…”

Section: Introductionmentioning

confidence: 99%

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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%

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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“…Zhao et al 46 found an amidase from A. niger W35 that degraded 85.1% of 2 μg/mL OTA within 12 h. The supernatant of B. subtilis CW14 contained carboxypeptidase DacB, which degraded 97.0% of 2 mg/mL OTA within 24 h 47 Additionally, Wei et al 31 reported that a new carboxypeptidase enzyme, cp4, from Lysobacterium CW239 degraded OTA by 36.8% at 0.25 mg/mL concentration. In a study by Chen et al, 48 Stenotrophomonas sp. CW117 amidohydrolase ADH3 enzyme degraded 60% of OTA at 0.1 mg/L concentration.…”

Section: Sequence Analysis Of the Purified Enzymesmentioning

confidence: 99%

“…Ochratoxin α (OTα) is known to be the main degradation products of OTA degradation. Similar findings have been reported in previous studies investigating other enzymes such as carboxypeptidase cp4, 31 hydrolase, 42 carboxypeptidase (ZHPCP), 58 amidase, 46 and N-acyl-L-amino acid amidohydrolase, 48 which have also demonstrated the ability to produce OTα. The result of this study suggested that Nh-9, Ce-3, and SP-3 may play a crucial role in OTA degradation in B. velezensis IS-6.…”

Section: Sequence Analysis Of the Purified Enzymesmentioning

confidence: 99%

Identification of a Novel Bacillus velezensis IS-6 Nudix Hydrolase Nh-9 Involved in Ochratoxin A Detoxification by Transcriptomic Profiling and Functional Verification

Jahan

Tai

et al. 2023

J. Agric. Food Chem.

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Contamination of foods and feeds with Ochratoxin A (OTA) is a global problem, and its detoxification is challenging. In this study, Bacillus velezensis IS-6 culture isolate supernatant degraded 1.5 g/mL OTA by 89% after 24 h of incubation at 37 °C, whereas viable cells and intra-cell extracts were less effective. The OTA degradation by B. velezensis IS-6 was an enzymatic process mediated by the culture supernatant. The degradation activity was optimal at 37 °C and pH 7.0, and Fe 2+ and Cu 2+ ions enhanced the OTA degradation. The LC−MS/MS analysis confirmed that structure of OTA was modified, resulting in the production of OTα that was less toxic than OTA. The transcriptomic analysis of B. velezensis IS-6 showed that 38 differentially expressed genes (DEGs) were significantly up-regulated, and 24 DEGs were down-regulated after treatment with OTA. A novel OTA degradation enzyme Nudix hydrolase Nh-9 was successfully cloned and characterized from the up-regulated genes. The recombinant Nh-9 enzyme was overexpressed in Escherichia coli BL21 and purified by affinity chromatography, exhibiting 68% degradation activity against 1.0 μg/ mL OTA at 37 °C in 24 h. The degraded product by the Nh-9 enzyme was identified as the less toxic OTα by LC−MS/MS. According to the findings, it can be inferred that Nh-9 is the main OTA-degrading enzyme in B. velezensis IS-6. Furthermore, OTA may be co-degraded by Nh-9, carboxylesterase, signal peptidase, and other degrading agents that are yet to be discovered in this strain.

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“…NAAs are present in tissue , and blood of mammalian . They function as pleiotropic bioactive lipids for nociception, bone function, , metabolism, , and neurodegeneration . Recently, several novel amino acid-conjugated bile acids were reported to agonize the farnesoid X receptor .…”

Section: Introductionmentioning

confidence: 99%

Discovery of N-Acyl Amino Acids and Novel Related N-, O-Acyl Lipids by Integrating Molecular Networking and an Extended In Silico Spectral Library

Yuan

et al. 2023

Anal. Chem.

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Research on novel bioactive lipids has garnered increasing interest. Although lipids can be identified by searching mass spectral libraries, the discovery of novel lipids remains challenging as the query spectra of such lipids are not included in libraries. In this study, we propose a strategy to discover novel carboxylic acid-containing acyl lipids by integrating molecular networking with an extended in silico spectral library. Derivatization was performed to improve the response of this method. The tandem mass spectrometry spectra enriched by derivatization facilitated the formation of molecular networking and 244 nodes were annotated. We constructed consensus spectra for these annotations based on molecular networking and developed an extended in silico spectral library based on these consensus spectra. The spectral library included 6879 in silico molecules covering 12,179 spectra. Using this integration strategy, 653 acyl lipids were discovered. Among these, O-acyl lactic acids and N-lactoyl amino acid-conjugated lipids were annotated as novel acyl lipids. Compared with conventional methods, our proposed method allows for the discovery of novel acyl lipids, and extended in silico libraries significantly increase the size of the spectral library.

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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

Abstract: Ochratoxin A (OTA) is a potent mycotoxin mainly produced by toxicogenic strains of Aspergillus spp. and seriously contaminates foods and feedstuffs. Previous OTA detoxification studies mainly focused on characterizations of degradation strains and detoxifying enzymes.

Cited by 13 publications

References 37 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

Identification of a Novel Bacillus velezensis IS-6 Nudix Hydrolase Nh-9 Involved in Ochratoxin A Detoxification by Transcriptomic Profiling and Functional Verification

Discovery of N-Acyl Amino Acids and Novel Related N-, O-Acyl Lipids by Integrating Molecular Networking and an Extended In Silico Spectral Library

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