Gene Cloning and Characterization of α-Glucuronidase of Bacillus stearothermophilus No. 236

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  • Gene Cloning and Characterization of .ALPHA.-Glucuronidase of Bacillus stearothermophilus. No. 236.
  • Gene Cloning and Characterization of アルファ Glucuronidase of Bacillus stearothermophilus No 236
  • Gene Cloning and Characterization of α-Glucuronidase of<i>Bacillus stearothermophilus</i>No. 236

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  The α-glucuronidase gene of Bacillus stearothermophilus No. 236 was cloned, sequenced, and expressed in Escherichia coli. The gene, designated aguA, encoded a 691-residue polypeptide with calculated molecular weight of 78,156 and pI of 5.34. The α-glucuronidase produced by a recombinant E. coli strain containing the aguA gene was purified to apparent homogeneity and characterized. The molecular weight of the α-glucuronidase was 77,000 by SDS-PAGE and 161,000 by gel filtration; the functional form of the α-glucuronidase therefore was dimeric. The optimal pH and temperature for the enzyme activity were pH 6.5 and 40°C, respectively. The enzyme's half-life at 50°C was 50 min. The values for the kinetic parameters of Km and Vmax were 0.78 mM and 15.3 U/mg for aldotriouronic acid [2-O-α- (4-O-methyl-α-D-glucopyranosyluronic)-D-xylobiose]. The α-glucuronidase acted mainly on small substituted xylo-oligomers and did not release methylglucuronic acid from intact xylan. Nevertheless, synergism in the release of xylose from xylan was found when α-glucuronidase was added to a mixture of endoxylanase and β-xylosidase.<br>

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