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National Institute of Environmental Health Sciences

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Publication Detail

Title: Characterization of a recombinant thermostable dehalogenase isolated from the hot spring thermophile Sulfolobus tokodaii.

Authors: Bachas-Daunert, Philip G; Law, Stacy A; Wei, Yinan

Published In Appl Biochem Biotechnol, (2009 Nov)

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.

PubMed ID: 19266316 Exiting the NIEHS site

MeSH Terms: No MeSH terms associated with this publication

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