Characterization of a recombinant thermostable dehalogenase isolated from the hot spring thermophile Sulfolobus tokodaii.
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.
Bachas-Daunert
Philip G
PG
Paul Laurence Dunbar High School, Lexington, KY 40513, USA.
Law
Stacy A
SA
Wei
Yinan
Y
D003001:Cloning, Molecular / Q000379:methods*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004926:Escherichia coli / Q000502:physiology; D045482:Hot Springs / Q000382:microbiology*; D006867:Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D016944:Sulfolobus / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism*; D013696:Temperature
D011994:Recombinant Proteins; D006867:Hydrolases; C034507:2-haloacid dehalogenase