Identification and characterization of Acinetobacter sp. CNU961 able to grow with phenol at high concentrations

An Acinetobacter sp., strain CNU961, with a higher tolerance to phenol was isolated, and identified through a set of taxonomic studies and a genetic complementation test. Enzymatic and mutagenic studies found that the strain dissimulate phenol by hydroxylation to catechol followed by an ortho-ring c...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1998, Vol.62 (9), p.1830-1833
Hauptverfasser: Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.)), Jeong, E.Y, Hwang, T.E, Choi, S.H
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 1833
container_issue 9
container_start_page 1830
container_title Bioscience, biotechnology, and biochemistry
container_volume 62
creator Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.))
Jeong, E.Y
Hwang, T.E
Choi, S.H
description An Acinetobacter sp., strain CNU961, with a higher tolerance to phenol was isolated, and identified through a set of taxonomic studies and a genetic complementation test. Enzymatic and mutagenic studies found that the strain dissimulate phenol by hydroxylation to catechol followed by an ortho-ring cleavage pathway to further mineralize it. The phenol hydroxylase, which is an inducible enzyme and requires NADPH for optimum activity, was not inhibited by phenol at concentrations up to 0.5 mM. The different kinetic behaviors of the enzyme activities on NADPH and on phenol reflected that the phenol hydroxylase of strain CNU961 is a multisubunit allosteric enzyme consisting of heterogeneous polypeptides
doi_str_mv 10.1271/bbb.62.1830
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_17291989</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3121825661</sourcerecordid><originalsourceid>FETCH-LOGICAL-c446t-19c9cfc16ea93a56ee1d35b4aab5b47b913648cf292e0d9291cb3dc0b22eac3</originalsourceid><addsrcrecordid>eNp90cFrFDEUBvAgil2rJ89KQCmCzJo3yWYmx7JYrRQV1HN4yWR2U2aTbTLLUv96s52tgoiXBB6_fEn4CHkObA51A--MMXNZz6Hl7AGZARdNJZVoHpIZUyCrVizghDzJ-ZqxMljAY3JSN1zVUvEZiZedC6PvvcXRx0AxdNSuMaEdXfI_p2Hs6bn1wY3R3M1p3s7p8vMPJYGiGRwdI12luKd7P67pdu1CHCiOdO1Xa2pjsOWKdBeVn5JHPQ7ZPTvup-Tbxfvvy4_V1ZcPl8vzq8oKIccKlFW2tyAdKo4L6Rx0fGEEoilrYxRwKVrb16p2rFO1Amt4Z5mpa4eWn5I3U-o2xZudy6Pe-GzdMGBwcZc1tIwL0ShQhZ79nzYlXLUH-OoveB13KZRPaBBCicJkU9TbSdkUc06u19vkN5huNTB9qEuXurSs9aGuol8eM3dm47rf9r6fAl4fAWaLQ58wWJ__ZEopJByYnJgPfUwb3Mc0dHrE2yGm-zP83w94MR3sMWpcpeI-fQWlFGPAmob_AldguEc</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1449429167</pqid></control><display><type>article</type><title>Identification and characterization of Acinetobacter sp. CNU961 able to grow with phenol at high concentrations</title><source>Oxford University Press Journals All Titles (1996-Current)</source><source>J-STAGE (Japan Science &amp; Technology Information Aggregator, Electronic) Freely Available Titles - Japanese</source><source>Open Access Titles of Japan</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.)) ; Jeong, E.Y ; Hwang, T.E ; Choi, S.H</creator><creatorcontrib>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.)) ; Jeong, E.Y ; Hwang, T.E ; Choi, S.H</creatorcontrib><description>An Acinetobacter sp., strain CNU961, with a higher tolerance to phenol was isolated, and identified through a set of taxonomic studies and a genetic complementation test. Enzymatic and mutagenic studies found that the strain dissimulate phenol by hydroxylation to catechol followed by an ortho-ring cleavage pathway to further mineralize it. The phenol hydroxylase, which is an inducible enzyme and requires NADPH for optimum activity, was not inhibited by phenol at concentrations up to 0.5 mM. The different kinetic behaviors of the enzyme activities on NADPH and on phenol reflected that the phenol hydroxylase of strain CNU961 is a multisubunit allosteric enzyme consisting of heterogeneous polypeptides</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.62.1830</identifier><identifier>PMID: 27392693</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>ACINETOBACTER ; Acinetobacter sp ; Bacteriology ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; catechol production ; COMPOSE PHENOLIQUE ; COMPUESTOS FENOLICOS ; Fundamental and applied biological sciences. Psychology ; IDENTIFICACION ; IDENTIFICATION ; Metabolism. Enzymes ; Microbiology ; Mission oriented research ; ortho-pathway ; phenol hydroxylase ; phenol tolerance ; PHENOLIC COMPOUNDS ; Physiology and metabolism</subject><ispartof>Bioscience, biotechnology, and biochemistry, 1998, Vol.62 (9), p.1830-1833</ispartof><rights>1998 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 1998</rights><rights>1999 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c446t-19c9cfc16ea93a56ee1d35b4aab5b47b913648cf292e0d9291cb3dc0b22eac3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=1664613$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27392693$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.))</creatorcontrib><creatorcontrib>Jeong, E.Y</creatorcontrib><creatorcontrib>Hwang, T.E</creatorcontrib><creatorcontrib>Choi, S.H</creatorcontrib><title>Identification and characterization of Acinetobacter sp. CNU961 able to grow with phenol at high concentrations</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>An Acinetobacter sp., strain CNU961, with a higher tolerance to phenol was isolated, and identified through a set of taxonomic studies and a genetic complementation test. Enzymatic and mutagenic studies found that the strain dissimulate phenol by hydroxylation to catechol followed by an ortho-ring cleavage pathway to further mineralize it. The phenol hydroxylase, which is an inducible enzyme and requires NADPH for optimum activity, was not inhibited by phenol at concentrations up to 0.5 mM. The different kinetic behaviors of the enzyme activities on NADPH and on phenol reflected that the phenol hydroxylase of strain CNU961 is a multisubunit allosteric enzyme consisting of heterogeneous polypeptides</description><subject>ACINETOBACTER</subject><subject>Acinetobacter sp</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>catechol production</subject><subject>COMPOSE PHENOLIQUE</subject><subject>COMPUESTOS FENOLICOS</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>IDENTIFICACION</subject><subject>IDENTIFICATION</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Mission oriented research</subject><subject>ortho-pathway</subject><subject>phenol hydroxylase</subject><subject>phenol tolerance</subject><subject>PHENOLIC COMPOUNDS</subject><subject>Physiology and metabolism</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNp90cFrFDEUBvAgil2rJ89KQCmCzJo3yWYmx7JYrRQV1HN4yWR2U2aTbTLLUv96s52tgoiXBB6_fEn4CHkObA51A--MMXNZz6Hl7AGZARdNJZVoHpIZUyCrVizghDzJ-ZqxMljAY3JSN1zVUvEZiZedC6PvvcXRx0AxdNSuMaEdXfI_p2Hs6bn1wY3R3M1p3s7p8vMPJYGiGRwdI12luKd7P67pdu1CHCiOdO1Xa2pjsOWKdBeVn5JHPQ7ZPTvup-Tbxfvvy4_V1ZcPl8vzq8oKIccKlFW2tyAdKo4L6Rx0fGEEoilrYxRwKVrb16p2rFO1Amt4Z5mpa4eWn5I3U-o2xZudy6Pe-GzdMGBwcZc1tIwL0ShQhZ79nzYlXLUH-OoveB13KZRPaBBCicJkU9TbSdkUc06u19vkN5huNTB9qEuXurSs9aGuol8eM3dm47rf9r6fAl4fAWaLQ58wWJ__ZEopJByYnJgPfUwb3Mc0dHrE2yGm-zP83w94MR3sMWpcpeI-fQWlFGPAmob_AldguEc</recordid><startdate>1998</startdate><enddate>1998</enddate><creator>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.))</creator><creator>Jeong, E.Y</creator><creator>Hwang, T.E</creator><creator>Choi, S.H</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><general>Oxford University Press</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>1998</creationdate><title>Identification and characterization of Acinetobacter sp. CNU961 able to grow with phenol at high concentrations</title><author>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.)) ; Jeong, E.Y ; Hwang, T.E ; Choi, S.H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-19c9cfc16ea93a56ee1d35b4aab5b47b913648cf292e0d9291cb3dc0b22eac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>ACINETOBACTER</topic><topic>Acinetobacter sp</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>catechol production</topic><topic>COMPOSE PHENOLIQUE</topic><topic>COMPUESTOS FENOLICOS</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>IDENTIFICACION</topic><topic>IDENTIFICATION</topic><topic>Metabolism. Enzymes</topic><topic>Microbiology</topic><topic>Mission oriented research</topic><topic>ortho-pathway</topic><topic>phenol hydroxylase</topic><topic>phenol tolerance</topic><topic>PHENOLIC COMPOUNDS</topic><topic>Physiology and metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.))</creatorcontrib><creatorcontrib>Jeong, E.Y</creatorcontrib><creatorcontrib>Hwang, T.E</creatorcontrib><creatorcontrib>Choi, S.H</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.))</au><au>Jeong, E.Y</au><au>Hwang, T.E</au><au>Choi, S.H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of Acinetobacter sp. CNU961 able to grow with phenol at high concentrations</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>1998</date><risdate>1998</risdate><volume>62</volume><issue>9</issue><spage>1830</spage><epage>1833</epage><pages>1830-1833</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>An Acinetobacter sp., strain CNU961, with a higher tolerance to phenol was isolated, and identified through a set of taxonomic studies and a genetic complementation test. Enzymatic and mutagenic studies found that the strain dissimulate phenol by hydroxylation to catechol followed by an ortho-ring cleavage pathway to further mineralize it. The phenol hydroxylase, which is an inducible enzyme and requires NADPH for optimum activity, was not inhibited by phenol at concentrations up to 0.5 mM. The different kinetic behaviors of the enzyme activities on NADPH and on phenol reflected that the phenol hydroxylase of strain CNU961 is a multisubunit allosteric enzyme consisting of heterogeneous polypeptides</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>27392693</pmid><doi>10.1271/bbb.62.1830</doi><tpages>4</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0916-8451
ispartof Bioscience, biotechnology, and biochemistry, 1998, Vol.62 (9), p.1830-1833
issn 0916-8451
1347-6947
language eng
recordid cdi_proquest_miscellaneous_17291989
source Oxford University Press Journals All Titles (1996-Current); J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Open Access Titles of Japan; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry
subjects ACINETOBACTER
Acinetobacter sp
Bacteriology
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
catechol production
COMPOSE PHENOLIQUE
COMPUESTOS FENOLICOS
Fundamental and applied biological sciences. Psychology
IDENTIFICACION
IDENTIFICATION
Metabolism. Enzymes
Microbiology
Mission oriented research
ortho-pathway
phenol hydroxylase
phenol tolerance
PHENOLIC COMPOUNDS
Physiology and metabolism
title Identification and characterization of Acinetobacter sp. CNU961 able to grow with phenol at high concentrations
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-03T20%3A42%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20and%20characterization%20of%20Acinetobacter%20sp.%20CNU961%20able%20to%20grow%20with%20phenol%20at%20high%20concentrations&rft.jtitle=Bioscience,%20biotechnology,%20and%20biochemistry&rft.au=Jeong,%20K.C.%20(Chonnam%20National%20Univ.,%20Kwangju%20(Korea%20R.))&rft.date=1998&rft.volume=62&rft.issue=9&rft.spage=1830&rft.epage=1833&rft.pages=1830-1833&rft.issn=0916-8451&rft.eissn=1347-6947&rft_id=info:doi/10.1271/bbb.62.1830&rft_dat=%3Cproquest_cross%3E3121825661%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1449429167&rft_id=info:pmid/27392693&rfr_iscdi=true