Loading…

Ochratoxin A degrading enzymes of Stenotrophomonas sp. 043-1a

Ochratoxin A is a secondary metabolite that acts as a mycotoxin and is produced by Aspergillus, Penicillium, and other fungal species. It is a threat to animal and human health due to nephrotoxic, carcinogenic, and genotoxic properties and its widespread incidence in agricultural products. To reduce...

Full description

Saved in:
Bibliographic Details
Published in:FEMS microbiology letters 2023-01, Vol.370
Main Authors: Gonaus, Christoph, Wieland, Laura, Thallinger, Gerhard G, Prasad, Shreenath
Format: Article
Language:English
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c169t-98b303839ebb9259437b7ac7a58f7938b2cfed277e8b0f1bcbb160a803793db3
cites cdi_FETCH-LOGICAL-c169t-98b303839ebb9259437b7ac7a58f7938b2cfed277e8b0f1bcbb160a803793db3
container_end_page
container_issue
container_start_page
container_title FEMS microbiology letters
container_volume 370
creator Gonaus, Christoph
Wieland, Laura
Thallinger, Gerhard G
Prasad, Shreenath
description Ochratoxin A is a secondary metabolite that acts as a mycotoxin and is produced by Aspergillus, Penicillium, and other fungal species. It is a threat to animal and human health due to nephrotoxic, carcinogenic, and genotoxic properties and its widespread incidence in agricultural products. To reduce this threat, biological remediation processes are of growing interest. The aerobic gram-negative bacterium Stenotrophomonassp. 043-1a, isolated from soil, was previously shown to degrade ochratoxin A into the non-toxic ochratoxin α and l-phenylalanine (Schatzmayr et al. 2002). However, the enzyme or enzymes catalyzing this reaction in this strain remained elusive. Here, we report the targeted purification of Stenotrophomonassp. 043-1a lysate via ammonium sulfate precipitation, size-exclusion chromatography, and hydrophobic interaction chromatography to identify the ochratoxin A degrading enzymes by subsequent peptide fragment fingerprinting. The metallo-dependent hydrolase Chr1_3858681_3267 and a member of the peptidase S9 family, Chr1_3858681_771, were shown to degrade ochratoxin A. This was, to our knowledge, the first report of an ochratoxin A degrading enzyme from the peptidase S9 family.
doi_str_mv 10.1093/femsle/fnad028
format article
fullrecord <record><control><sourceid>crossref</sourceid><recordid>TN_cdi_crossref_primary_10_1093_femsle_fnad028</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>10_1093_femsle_fnad028</sourcerecordid><originalsourceid>FETCH-LOGICAL-c169t-98b303839ebb9259437b7ac7a58f7938b2cfed277e8b0f1bcbb160a803793db3</originalsourceid><addsrcrecordid>eNpNz8FLwzAYBfAgCs7p1XP-gXZfkrZJDh7GcCoMdnD3kqRftsqalKQH51_vZDt4eg8ePPgR8sygZKDFwuOQj7jwwXTA1Q2ZsVpWRaMbdfuv35OHnL8AoOLQzMjL1h2SmeJ3H-iSdrhPpuvDnmL4OQ2YafT0c8IQpxTHQxxiMJnmsaRQiYKZR3LnzTHj0zXnZLd-3a3ei8327WO13BSONXoqtLIChBIardW81pWQVhonTa281EJZ7jx2XEpUFjyzzlrWgFEgzmtnxZyUl1uXYs4JfTumfjDp1DJo_-ztxd5e7eIX7ktO9g</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Ochratoxin A degrading enzymes of Stenotrophomonas sp. 043-1a</title><source>Oxford Journals Online</source><creator>Gonaus, Christoph ; Wieland, Laura ; Thallinger, Gerhard G ; Prasad, Shreenath</creator><creatorcontrib>Gonaus, Christoph ; Wieland, Laura ; Thallinger, Gerhard G ; Prasad, Shreenath</creatorcontrib><description>Ochratoxin A is a secondary metabolite that acts as a mycotoxin and is produced by Aspergillus, Penicillium, and other fungal species. It is a threat to animal and human health due to nephrotoxic, carcinogenic, and genotoxic properties and its widespread incidence in agricultural products. To reduce this threat, biological remediation processes are of growing interest. The aerobic gram-negative bacterium Stenotrophomonassp. 043-1a, isolated from soil, was previously shown to degrade ochratoxin A into the non-toxic ochratoxin α and l-phenylalanine (Schatzmayr et al. 2002). However, the enzyme or enzymes catalyzing this reaction in this strain remained elusive. Here, we report the targeted purification of Stenotrophomonassp. 043-1a lysate via ammonium sulfate precipitation, size-exclusion chromatography, and hydrophobic interaction chromatography to identify the ochratoxin A degrading enzymes by subsequent peptide fragment fingerprinting. The metallo-dependent hydrolase Chr1_3858681_3267 and a member of the peptidase S9 family, Chr1_3858681_771, were shown to degrade ochratoxin A. This was, to our knowledge, the first report of an ochratoxin A degrading enzyme from the peptidase S9 family.</description><identifier>ISSN: 1574-6968</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1093/femsle/fnad028</identifier><language>eng</language><ispartof>FEMS microbiology letters, 2023-01, Vol.370</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c169t-98b303839ebb9259437b7ac7a58f7938b2cfed277e8b0f1bcbb160a803793db3</citedby><cites>FETCH-LOGICAL-c169t-98b303839ebb9259437b7ac7a58f7938b2cfed277e8b0f1bcbb160a803793db3</cites><orcidid>0000-0003-2475-8089 ; 0000-0002-2864-5404</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids></links><search><creatorcontrib>Gonaus, Christoph</creatorcontrib><creatorcontrib>Wieland, Laura</creatorcontrib><creatorcontrib>Thallinger, Gerhard G</creatorcontrib><creatorcontrib>Prasad, Shreenath</creatorcontrib><title>Ochratoxin A degrading enzymes of Stenotrophomonas sp. 043-1a</title><title>FEMS microbiology letters</title><description>Ochratoxin A is a secondary metabolite that acts as a mycotoxin and is produced by Aspergillus, Penicillium, and other fungal species. It is a threat to animal and human health due to nephrotoxic, carcinogenic, and genotoxic properties and its widespread incidence in agricultural products. To reduce this threat, biological remediation processes are of growing interest. The aerobic gram-negative bacterium Stenotrophomonassp. 043-1a, isolated from soil, was previously shown to degrade ochratoxin A into the non-toxic ochratoxin α and l-phenylalanine (Schatzmayr et al. 2002). However, the enzyme or enzymes catalyzing this reaction in this strain remained elusive. Here, we report the targeted purification of Stenotrophomonassp. 043-1a lysate via ammonium sulfate precipitation, size-exclusion chromatography, and hydrophobic interaction chromatography to identify the ochratoxin A degrading enzymes by subsequent peptide fragment fingerprinting. The metallo-dependent hydrolase Chr1_3858681_3267 and a member of the peptidase S9 family, Chr1_3858681_771, were shown to degrade ochratoxin A. This was, to our knowledge, the first report of an ochratoxin A degrading enzyme from the peptidase S9 family.</description><issn>1574-6968</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNpNz8FLwzAYBfAgCs7p1XP-gXZfkrZJDh7GcCoMdnD3kqRftsqalKQH51_vZDt4eg8ePPgR8sygZKDFwuOQj7jwwXTA1Q2ZsVpWRaMbdfuv35OHnL8AoOLQzMjL1h2SmeJ3H-iSdrhPpuvDnmL4OQ2YafT0c8IQpxTHQxxiMJnmsaRQiYKZR3LnzTHj0zXnZLd-3a3ei8327WO13BSONXoqtLIChBIardW81pWQVhonTa281EJZ7jx2XEpUFjyzzlrWgFEgzmtnxZyUl1uXYs4JfTumfjDp1DJo_-ztxd5e7eIX7ktO9g</recordid><startdate>20230117</startdate><enddate>20230117</enddate><creator>Gonaus, Christoph</creator><creator>Wieland, Laura</creator><creator>Thallinger, Gerhard G</creator><creator>Prasad, Shreenath</creator><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0003-2475-8089</orcidid><orcidid>https://orcid.org/0000-0002-2864-5404</orcidid></search><sort><creationdate>20230117</creationdate><title>Ochratoxin A degrading enzymes of Stenotrophomonas sp. 043-1a</title><author>Gonaus, Christoph ; Wieland, Laura ; Thallinger, Gerhard G ; Prasad, Shreenath</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c169t-98b303839ebb9259437b7ac7a58f7938b2cfed277e8b0f1bcbb160a803793db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gonaus, Christoph</creatorcontrib><creatorcontrib>Wieland, Laura</creatorcontrib><creatorcontrib>Thallinger, Gerhard G</creatorcontrib><creatorcontrib>Prasad, Shreenath</creatorcontrib><collection>CrossRef</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gonaus, Christoph</au><au>Wieland, Laura</au><au>Thallinger, Gerhard G</au><au>Prasad, Shreenath</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ochratoxin A degrading enzymes of Stenotrophomonas sp. 043-1a</atitle><jtitle>FEMS microbiology letters</jtitle><date>2023-01-17</date><risdate>2023</risdate><volume>370</volume><issn>1574-6968</issn><eissn>1574-6968</eissn><abstract>Ochratoxin A is a secondary metabolite that acts as a mycotoxin and is produced by Aspergillus, Penicillium, and other fungal species. It is a threat to animal and human health due to nephrotoxic, carcinogenic, and genotoxic properties and its widespread incidence in agricultural products. To reduce this threat, biological remediation processes are of growing interest. The aerobic gram-negative bacterium Stenotrophomonassp. 043-1a, isolated from soil, was previously shown to degrade ochratoxin A into the non-toxic ochratoxin α and l-phenylalanine (Schatzmayr et al. 2002). However, the enzyme or enzymes catalyzing this reaction in this strain remained elusive. Here, we report the targeted purification of Stenotrophomonassp. 043-1a lysate via ammonium sulfate precipitation, size-exclusion chromatography, and hydrophobic interaction chromatography to identify the ochratoxin A degrading enzymes by subsequent peptide fragment fingerprinting. The metallo-dependent hydrolase Chr1_3858681_3267 and a member of the peptidase S9 family, Chr1_3858681_771, were shown to degrade ochratoxin A. This was, to our knowledge, the first report of an ochratoxin A degrading enzyme from the peptidase S9 family.</abstract><doi>10.1093/femsle/fnad028</doi><orcidid>https://orcid.org/0000-0003-2475-8089</orcidid><orcidid>https://orcid.org/0000-0002-2864-5404</orcidid></addata></record>
fulltext fulltext
identifier ISSN: 1574-6968
ispartof FEMS microbiology letters, 2023-01, Vol.370
issn 1574-6968
1574-6968
language eng
recordid cdi_crossref_primary_10_1093_femsle_fnad028
source Oxford Journals Online
title Ochratoxin A degrading enzymes of Stenotrophomonas sp. 043-1a
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-23T12%3A12%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-crossref&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Ochratoxin%20A%20degrading%20enzymes%20of%20Stenotrophomonas%20sp.%20043-1a&rft.jtitle=FEMS%20microbiology%20letters&rft.au=Gonaus,%20Christoph&rft.date=2023-01-17&rft.volume=370&rft.issn=1574-6968&rft.eissn=1574-6968&rft_id=info:doi/10.1093/femsle/fnad028&rft_dat=%3Ccrossref%3E10_1093_femsle_fnad028%3C/crossref%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c169t-98b303839ebb9259437b7ac7a58f7938b2cfed277e8b0f1bcbb160a803793db3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true