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Appl. Environ. Microbiol., Mar 1995, 1077-1081, Vol 61, No. 3
Copyright © 1995, American Society for Microbiology

Purification and Characterization of the (alpha)-Glucuronidase from Thermoanaerobacterium sp. Strain JW/SL-YS485, an Important Enzyme for the Utilization of Substituted Xylans

W Shao, SKC Obi, J Puls and J Wiegel
Department of Microbiology and Center for Biological Resource Recovery, University of Georgia, Athens, Georgia 30602, and Institute fur Holzchemie, Bundesforschungsanstalt, Hamburg, Germany

A cell-associated (alpha)-glucuronidase was purified to gel electrophoretic homogeneity from the thermophilic anaerobic bacterium Thermoanaerobacterium sp. strain JW/SL-YS485. This enzyme had a pI of 4.65, a molecular weight of 130,000, and two subunits; the molecular weight of each subunit was 74,000. The enzyme exhibited the highest level of activity at pH 5.4 and 60(deg)C, as determined by a 5-min assay. The K(infm) and k(infcat) values of the enzyme for 4-methylglucuronosyl xylobiose were 0.76 mM and 1,083 IU/(mu)mol, respectively. The Arrhenius energy was 26.4 kJ/mol. The specific activities of the enzyme with 4-O-methylglucuronosyl xylobiose, 4-O-methylglucuronosyl xylotriose, and 4-O-methylglucuronosyl xylotetraose were 8.4, 4.8, and 3.9 IU/mg, respectively. The purified (alpha)-glucuronidase and a (beta)-xylosidase purified from the same organism interacted synergistically to hydrolyze 4-methylglucuronosyl xylotetraose.

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