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

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Title: Purification and characterization of an intracellular esterase from a Fusarium species capable of degrading dimethyl terephthalate
Authors: Luo, Zhu-Hua1,2 luozhuhua@hotmail.com, Wu, Yi-Rui2,3, Chow, R.K.K.2, Luo, Jing-Jing1, Gu, Ji-Dong4, Vrijmoed, L.L.P.2 bhlilian@cityu.edu.hk
Source: Process Biochemistry. May2012, Vol. 47 Issue 5, p687-693. 7p.
Subjects: Esterases, Fusarium, Dimethyl terephthalate, Biodegradation, Phthalate esters, Linkage (Genetics), Enzymatic analysis
Abstract: Abstract: Esterase 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 84kDa. 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 Cr3+, Hg2+, Cu2+, Zn2+, Ni2+, and Cd2+. 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. [Copyright &y& Elsevier]
Copyright of Process Biochemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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Header DbId: egs
DbLabel: Engineering Source
An: 74096657
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
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  Data: Purification and characterization of an intracellular esterase from a Fusarium species capable of degrading dimethyl terephthalate
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  Data: <searchLink fieldCode="AR" term="%22Luo%2C+Zhu-Hua%22">Luo, Zhu-Hua</searchLink><relatesTo>1,2</relatesTo><i> luozhuhua@hotmail.com</i><br /><searchLink fieldCode="AR" term="%22Wu%2C+Yi-Rui%22">Wu, Yi-Rui</searchLink><relatesTo>2,3</relatesTo><br /><searchLink fieldCode="AR" term="%22Chow%2C+R%2EK%2EK%2E%22">Chow, R.K.K.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Luo%2C+Jing-Jing%22">Luo, Jing-Jing</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Gu%2C+Ji-Dong%22">Gu, Ji-Dong</searchLink><relatesTo>4</relatesTo><br /><searchLink fieldCode="AR" term="%22Vrijmoed%2C+L%2EL%2EP%2E%22">Vrijmoed, L.L.P.</searchLink><relatesTo>2</relatesTo><i> bhlilian@cityu.edu.hk</i>
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  Data: <searchLink fieldCode="JN" term="%22Process+Biochemistry%22">Process Biochemistry</searchLink>. May2012, Vol. 47 Issue 5, p687-693. 7p.
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  Data: <searchLink fieldCode="DE" term="%22Esterases%22">Esterases</searchLink><br /><searchLink fieldCode="DE" term="%22Fusarium%22">Fusarium</searchLink><br /><searchLink fieldCode="DE" term="%22Dimethyl+terephthalate%22">Dimethyl terephthalate</searchLink><br /><searchLink fieldCode="DE" term="%22Biodegradation%22">Biodegradation</searchLink><br /><searchLink fieldCode="DE" term="%22Phthalate+esters%22">Phthalate esters</searchLink><br /><searchLink fieldCode="DE" term="%22Linkage+%28Genetics%29%22">Linkage (Genetics)</searchLink><br /><searchLink fieldCode="DE" term="%22Enzymatic+analysis%22">Enzymatic analysis</searchLink>
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  Data: Abstract: Esterase 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 84kDa. 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 Cr3+, Hg2+, Cu2+, Zn2+, Ni2+, and Cd2+. 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. [Copyright &y& Elsevier]
– Name: AbstractSuppliedCopyright
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  Data: <i>Copyright of Process Biochemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1016/j.procbio.2012.01.015
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        Text: English
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      – SubjectFull: Fusarium
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      – SubjectFull: Dimethyl terephthalate
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      – SubjectFull: Biodegradation
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      – SubjectFull: Linkage (Genetics)
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      – SubjectFull: Enzymatic analysis
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              Text: May2012
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