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
en Zh
| WPRIM
| ID: wpr-275370
Biblioteca responsable:
WPRO
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.
Texto completo:
1
Base de datos:
WPRIM
Asunto principal:
Estabilidad de Enzimas
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Proteínas Recombinantes
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Cinética
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Clonación Molecular
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Ácido Glicirrínico
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Thermotoga maritima
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Escherichia coli
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Genética
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Glucuronidasa
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Ácido Glicirretínico
Idioma:
Zh
Revista:
Chinese Journal of Biotechnology
Año:
2008
Tipo del documento:
Article