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Mode of action and properties of the β-xylosidases from Talaromyces emersonii and Trichoderma reesei by Louise E. Rasmussen; Hanne R. Sørensen; Jesper Vind; Anders Viksø-Nielsen is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Enzymatic hydrolysis of arabinoxylan is an important prerequisite for the utilization of hemicellulose for ethanol fermentation or for making the low calorie sweetener xylitol by catalytic hydrogenation of the generated xylose. This study focus on cloning and characterization of two industrial relevant b-xylosidases (1,4-b-D-xylan xylohydrolase, EC 3.2.1.37) from Talaromyces emersonii (bXTE) and Trichoderma reesei (bXTR) and a comparison of these in relation to hemicellulose hydrolysis using an industrial relevant substrate. Both bxylosidases were expressed in A. oryzae and subsequently purified. During the enzymatic hydrolysis of xylobiose, the reaction product of both enzymes was found to be b-D-xylose proving that the hydrolysis is proceeding via a retaining reaction mechanism. Based on sequence similarities and glycosyl hydrolases family membership, the active site residues of bXTE and bXTR are predicted to be Asp 242 and Glu 441, and Asp 264 and Glu 464, respectively. The involvement in catalysis of these carboxyls was examined by modification using the carbodiimide-nucleophile procedure resulting in a complete inactivation of both enzymes. The degree of xylose release from vi

Who reads Mode of action and properties of the β-xylosidases from Talaromyces emersonii and Trichoderma reesei?

Author

Louise E. Rasmussen; Hanne R. Sørensen; Jesper Vind; Anders Viksø-Nielsen

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley - V C H Verlag GmbbH & Co.; Wiley (ISSN 0006-3592)

Published

2006

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)