Expression, characterization and application of thermostable beta-glucuronidase from Thermotoga maritima / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 1407-1412, 2008.
Article
in Chinese
| WPRIM
| ID: wpr-275370
ABSTRACT
The gene of beta-glucuronidase from Thermotoga maritima was cloned into the plasmid pHsh, and expressed in Escherichia coli JM109. The recombinant protein was purified to homogeneity by a simple step, heat treatment. The recombinant enzyme had a molecular mass of 65.9 kD. The optimal activity of beta-glucuronidase was found at pH 5.0 and 80 degrees C. The purified enzyme was stable over a pH range from 5.8 to 8.2 and had a half life of 2 h at 80 degrees C. The kinetic experiments at 80 degrees C with p-nitrophenyl-beta- glucuronide as substrate gave a K(m) and V(max) of 0.18 mmol/L and 312 u per mg of protein. The purified enzyme could transform glycyrrhizin to glycyrrhetinic acid.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Enzyme Stability
/
Recombinant Proteins
/
Kinetics
/
Cloning, Molecular
/
Glycyrrhizic Acid
/
Thermotoga maritima
/
Escherichia coli
/
Genetics
/
Glucuronidase
/
Glycyrrhetinic Acid
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2008
Type:
Article
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