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Characterization of a highly efficient heterodimeric xylosidase from Humicola insolens

Paper ID Volume ID Publish Year Pages File Format Full-Text
17419 42667 2009 7 PDF Available
Title
Characterization of a highly efficient heterodimeric xylosidase from Humicola insolens
Abstract

A heterodimeric xylosidase (E.C. 3.2.1.37) with robust activity is secreted among the plant cell wall degrading enzymes produced by the saprophytic fungus Humicola insolens. The xylosidase has been purified to homogeneity by gel filtration and cation exchange chromatography, and demonstrated to be composed of two protein subunits of 68 and 17 kDa with a molecular mass in solution of approximately 85 kDa based on a combination of SDS-PAGE, size exclusion chromatography and analytical ultracentrifugation. Peptide sequence identities from the subunits indicate the 68 kDa subunit contains a catalytic protein domain and the 17 kDa subunit a carbohydrate binding module. The xylosidase has wide biotechnological potential with maximum activity exhibited at 70 °C and kinetic constants with p-nitrophenol xylopyranoside substrate that suggest it has the highest catalytic efficiency recorded to date (Vmax 22.17 μmoles/min/mg, Km 1.74 mM and Kcat 6787/s).

Keywords
Xylosidase; Xylan digestion; Bioenergy; Biorefining; Humicola; Plant cell wall digestion
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Characterization of a highly efficient heterodimeric xylosidase from Humicola insolens
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 45, Issues 6–7, December 2009, Pages 436–442
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
Online Support
Any Questions? feel free to contact us