Characterization of a recombinant thermostable dehalogenase isolated from the hot spring thermophile sulfolobus tokodaii

Philip G. Bachas-Daunert; Stacy A. Law; Yinan Wei

doi:10.1007/s12010-009-8589-9

Characterization of a recombinant thermostable dehalogenase isolated from the hot spring thermophile sulfolobus tokodaii

Philip G. Bachas-Daunert
, Stacy A. Law
, Yinan Wei

Chemistry

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

11 Scopus citations

Abstract

A putative dehalogenase, l-HAD_ST, from the thermophile Sulfolobus tokodaii, was cloned and expressed in Escherichia coli. The recombinant enzyme catalyzes the stereospecific dehalogenation of l-2-haloacids with similar levels of activity as its homolog from mesophiles. l-HAD _ST remains fully active after being incubated for 4 h at 70 °C and tolerates extreme pH conditions ranging from 4 to 10. Furthermore, it can be purified conveniently without the usage of any chromatography method. The high expression yield and easy purification procedure make the recombinant dehalogenase an excellent candidate for biotechnological applications.

Original language	English
Pages (from-to)	382-393
Number of pages	12
Journal	Applied Biochemistry and Biotechnology
Volume	159
Issue number	2
DOIs	https://doi.org/10.1007/s12010-009-8589-9
State	Published - Nov 2009

Bibliographical note

Funding Information:
Acknowledgment This work was supported by the National Institute of Environmental Health Sciences (NIH, grant P42 ES07380). We acknowledge the use of the circular dichroism spectrometer at the Protein Core facility housed in the Department of Molecular and Cellular Biochemistry, University of Kentucky and directed by Dr. David Rodgers.

Funding

Acknowledgment This work was supported by the National Institute of Environmental Health Sciences (NIH, grant P42 ES07380). We acknowledge the use of the circular dichroism spectrometer at the Protein Core facility housed in the Department of Molecular and Cellular Biochemistry, University of Kentucky and directed by Dr. David Rodgers.

Funders	Funder number
National Institute of Environmental Health Sciences (NIEHS)	P42ES007380

Keywords

Extremophile
L-2 Haloacid dehalogenase
Recombinant
Thermostable

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology

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10.1007/s12010-009-8589-9

Cite this

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title = "Characterization of a recombinant thermostable dehalogenase isolated from the hot spring thermophile sulfolobus tokodaii",

abstract = "A putative dehalogenase, l-HADST, from the thermophile Sulfolobus tokodaii, was cloned and expressed in Escherichia coli. The recombinant enzyme catalyzes the stereospecific dehalogenation of l-2-haloacids with similar levels of activity as its homolog from mesophiles. l-HAD ST remains fully active after being incubated for 4 h at 70 °C and tolerates extreme pH conditions ranging from 4 to 10. Furthermore, it can be purified conveniently without the usage of any chromatography method. The high expression yield and easy purification procedure make the recombinant dehalogenase an excellent candidate for biotechnological applications.",

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author = "Bachas-Daunert, \{Philip G.\} and Law, \{Stacy A.\} and Yinan Wei",

note = "Funding Information: Acknowledgment This work was supported by the National Institute of Environmental Health Sciences (NIH, grant P42 ES07380). We acknowledge the use of the circular dichroism spectrometer at the Protein Core facility housed in the Department of Molecular and Cellular Biochemistry, University of Kentucky and directed by Dr. David Rodgers.",

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AU - Bachas-Daunert, Philip G.

AU - Law, Stacy A.

AU - Wei, Yinan

N1 - Funding Information: Acknowledgment This work was supported by the National Institute of Environmental Health Sciences (NIH, grant P42 ES07380). We acknowledge the use of the circular dichroism spectrometer at the Protein Core facility housed in the Department of Molecular and Cellular Biochemistry, University of Kentucky and directed by Dr. David Rodgers.

PY - 2009/11

Y1 - 2009/11

N2 - A putative dehalogenase, l-HADST, from the thermophile Sulfolobus tokodaii, was cloned and expressed in Escherichia coli. The recombinant enzyme catalyzes the stereospecific dehalogenation of l-2-haloacids with similar levels of activity as its homolog from mesophiles. l-HAD ST remains fully active after being incubated for 4 h at 70 °C and tolerates extreme pH conditions ranging from 4 to 10. Furthermore, it can be purified conveniently without the usage of any chromatography method. The high expression yield and easy purification procedure make the recombinant dehalogenase an excellent candidate for biotechnological applications.

AB - A putative dehalogenase, l-HADST, from the thermophile Sulfolobus tokodaii, was cloned and expressed in Escherichia coli. The recombinant enzyme catalyzes the stereospecific dehalogenation of l-2-haloacids with similar levels of activity as its homolog from mesophiles. l-HAD ST remains fully active after being incubated for 4 h at 70 °C and tolerates extreme pH conditions ranging from 4 to 10. Furthermore, it can be purified conveniently without the usage of any chromatography method. The high expression yield and easy purification procedure make the recombinant dehalogenase an excellent candidate for biotechnological applications.

KW - Extremophile

KW - L-2 Haloacid dehalogenase

KW - Recombinant

KW - Thermostable

UR - https://www.scopus.com/pages/publications/70350634259

UR - https://www.scopus.com/pages/publications/70350634259#tab=citedBy

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DO - 10.1007/s12010-009-8589-9

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C2 - 19266316

AN - SCOPUS:70350634259

SN - 0273-2289

VL - 159

SP - 382

EP - 393

JO - Applied Biochemistry and Biotechnology

JF - Applied Biochemistry and Biotechnology

IS - 2

ER -

Characterization of a recombinant thermostable dehalogenase isolated from the hot spring thermophile sulfolobus tokodaii

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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