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  • Title: [Expression, characterization and application of thermostable beta-glucuronidase from Thermotoga maritima].
    Author: Wang Z, Pei J, Li H, Shao W.
    Journal: Sheng Wu Gong Cheng Xue Bao; 2008 Aug; 24(8):1407-12. PubMed ID: 18998543.
    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.
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