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

Zhu Hua Luo; Yi Rui Wu; R. K.K. Chow; Jing Jing Luo; Ji Dong Gu; L. L.P. Vrijmoed

doi:10.1016/j.procbio.2012.01.015

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

Zhu Hua Luo^*, Yi Rui Wu, R. K.K. Chow, Jing Jing Luo, Ji Dong Gu, L. L.P. Vrijmoed

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

48 Scopus citations

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 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.

Original language	English
Pages (from-to)	687-693
Number of pages	7
Journal	Process Biochemistry
Volume	47
Issue number	5
DOIs	https://doi.org/10.1016/j.procbio.2012.01.015
State	Published - May 2012
Externally published	Yes

Keywords

Degradation
Esterase
Fusarium sp.
Phthalate esters (PAEs)

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10.1016/j.procbio.2012.01.015

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@article{42037e58ae904d2c82d6868e2d74971b,

title = "Purification and characterization of an intracellular esterase from a Fusarium species capable of degrading dimethyl terephthalate",

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 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.",

keywords = "Degradation, Esterase, Fusarium sp., Phthalate esters (PAEs)",

author = "Luo, {Zhu Hua} and Wu, {Yi Rui} and Chow, {R. K.K.} and Luo, {Jing Jing} and Gu, {Ji Dong} and Vrijmoed, {L. L.P.}",

note = "Funding Information: The work described in this paper was substantially supported by grants from National Natural Science Foundation of China (Project No. 41006099), City University of Hong Kong (Project No. 7002220 and 9610037), and the Research Grants Council of the Hong Kong Special Administrative Region, China (Project No. CA04/05. SC01), which are gratefully acknowledged. The authors would also like to thank Miss Alice Chan of City University of Hong Kong for technical support in HPLC analysis.",

year = "2012",

month = may,

doi = "10.1016/j.procbio.2012.01.015",

language = "英语",

volume = "47",

pages = "687--693",

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AU - Luo, Zhu Hua

AU - Wu, Yi Rui

AU - Chow, R. K.K.

AU - Luo, Jing Jing

AU - Gu, Ji Dong

AU - Vrijmoed, L. L.P.

N1 - Funding Information: The work described in this paper was substantially supported by grants from National Natural Science Foundation of China (Project No. 41006099), City University of Hong Kong (Project No. 7002220 and 9610037), and the Research Grants Council of the Hong Kong Special Administrative Region, China (Project No. CA04/05. SC01), which are gratefully acknowledged. The authors would also like to thank Miss Alice Chan of City University of Hong Kong for technical support in HPLC analysis.

PY - 2012/5

Y1 - 2012/5

N2 - 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 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.

AB - 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 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.

KW - Degradation

KW - Esterase

KW - Fusarium sp.

KW - Phthalate esters (PAEs)

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DO - 10.1016/j.procbio.2012.01.015

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SN - 1359-5113

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EP - 693

JO - Process Biochemistry

JF - Process Biochemistry

IS - 5

ER -

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

Abstract

Keywords

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