Characterization of a recombinant thermostable dehalogenase isolated from the hot spring thermophile Sulfolobus tokodaii. Academic Article

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 degrees 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.

authors

• Wei, Yinan

published proceedings

• Appl Biochem Biotechnol

altmetric score

• 9

author list (cited authors)

• Bachas-Daunert, P. G., Law, S. A., & Wei, Y.

citation count

• 6

complete list of authors

• Bachas-Daunert, Philip G||Law, Stacy A||Wei, Yinan

publication date

• November 2009

publisher

• Springer Nature  Publisher

published in

• Applied Biochemistry and Biotechnology  Journal

keywords

• Cloning, Molecular
• Enzyme Activation
• Enzyme Stability
• Escherichia Coli
• Hot Springs
• Hydrolases
• Protein Engineering
• Recombinant Proteins
• Sulfolobus
• Temperature

PubMed Central ID

• 19266316

Digital Object Identifier (DOI)

• 10.1007/s12010-009-8589-9

start page

• 382

end page

• 393

volume

• 159

issue

• 2

URL

• http://dx.doi.org/10.1007/s12010-009-8589-9