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Article: Purification and characterization of an intracellular esterase from a Fusarium species capable of degrading dimethyl terephthalate

TitlePurification and characterization of an intracellular esterase from a Fusarium species capable of degrading dimethyl terephthalate
Authors
KeywordsCarboxylic esters
Coastal sediments
Dimethyl phthalate
Dimethyl terephthalate
Esterase activities
Issue Date2012
PublisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/procbio
Citation
Process Biochemistry, 2012, v. 47 n. 5, p. 687-693 How to Cite?
AbstractEsterase is the key enzyme involved in microbial degradation of phthalate esters (PAEs). In this study, an intracellular esterase was purified from a coastal sediment fungus Fusarium sp. DMT-5-3 capable of utilizing dimethyl terephthalate (DMT) as a substrate. The purified enzyme is a polymeric protein consisting of two identical subunits with a molecular mass of about 84 kDa. The enzyme showed a maximum esterase activity at 50 °C and was stable below 30 °C. The optimal pH was 8.0 and the enzyme was stable between pH 6.0 and 10.0. The esterase activity was inhibited by Cr 3+, Hg 2+, Cu 2+, Zn 2+, Ni 2+, and Cd 2+. Substrate specificity analysis showed that the enzyme was specific to DMT hydrolysis, but had no effect on other isomers of dimethyl phthalate esters (DMPEs) or monomethyl phthalate esters (MMPEs). These findings suggest that the phthalate esterase produced by Fusarium sp. DMT-5-3 is inducible and distinctive esterases involved in hydrolysis of the two carboxylic ester linkages of DMPEs. © 2012 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/165967
ISSN
2015 Impact Factor: 2.529
2015 SCImago Journal Rankings: 0.937
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLuo, ZHen_HK
dc.contributor.authorWu, YRen_HK
dc.contributor.authorChow, RKKen_HK
dc.contributor.authorLuo, JJen_HK
dc.contributor.authorGu, JDen_HK
dc.contributor.authorVrijmoed, LLPen_HK
dc.date.accessioned2012-09-20T08:25:53Z-
dc.date.available2012-09-20T08:25:53Z-
dc.date.issued2012en_HK
dc.identifier.citationProcess Biochemistry, 2012, v. 47 n. 5, p. 687-693en_HK
dc.identifier.issn1359-5113en_HK
dc.identifier.urihttp://hdl.handle.net/10722/165967-
dc.description.abstractEsterase is the key enzyme involved in microbial degradation of phthalate esters (PAEs). In this study, an intracellular esterase was purified from a coastal sediment fungus Fusarium sp. DMT-5-3 capable of utilizing dimethyl terephthalate (DMT) as a substrate. The purified enzyme is a polymeric protein consisting of two identical subunits with a molecular mass of about 84 kDa. The enzyme showed a maximum esterase activity at 50 °C and was stable below 30 °C. The optimal pH was 8.0 and the enzyme was stable between pH 6.0 and 10.0. The esterase activity was inhibited by Cr 3+, Hg 2+, Cu 2+, Zn 2+, Ni 2+, and Cd 2+. Substrate specificity analysis showed that the enzyme was specific to DMT hydrolysis, but had no effect on other isomers of dimethyl phthalate esters (DMPEs) or monomethyl phthalate esters (MMPEs). These findings suggest that the phthalate esterase produced by Fusarium sp. DMT-5-3 is inducible and distinctive esterases involved in hydrolysis of the two carboxylic ester linkages of DMPEs. © 2012 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_US
dc.publisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/procbioen_HK
dc.relation.ispartofProcess Biochemistryen_HK
dc.subjectCarboxylic estersen_HK
dc.subjectCoastal sedimentsen_HK
dc.subjectDimethyl phthalateen_HK
dc.subjectDimethyl terephthalateen_HK
dc.subjectEsterase activities-
dc.titlePurification and characterization of an intracellular esterase from a Fusarium species capable of degrading dimethyl terephthalateen_HK
dc.typeArticleen_HK
dc.identifier.emailLuo, ZH: luozhuhua@hotmail.comen_HK
dc.identifier.emailGu, JD: jdgu@hkucc.hku.hk-
dc.identifier.emailVrijmoed, LLP: bhlilian@cityu.edu.hk-
dc.identifier.authorityGu, JD=rp00701en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.procbio.2012.01.015en_HK
dc.identifier.scopuseid_2-s2.0-84862823216en_HK
dc.identifier.hkuros209709en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84862823216&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume47en_HK
dc.identifier.issue5en_HK
dc.identifier.spage687en_HK
dc.identifier.epage693en_HK
dc.identifier.isiWOS:000303622400002-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridVrijmoed, LLP=7003337180en_HK
dc.identifier.scopusauthoridGu, JD=7403129601en_HK
dc.identifier.scopusauthoridLuo, JJ=55262405500en_HK
dc.identifier.scopusauthoridChow, RKK=36845171200en_HK
dc.identifier.scopusauthoridWu, YR=36195002000en_HK
dc.identifier.scopusauthoridLuo, ZH=35206114900en_HK

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