Purification and characterization of an alpha-D-glucuronidase from a thermophilic fungus, Thermoascus aurantiacus

Khandke, Kiran M and Vithayathil, PJ and Murthy, SK (1989) Purification and characterization of an alpha-D-glucuronidase from a thermophilic fungus, Thermoascus aurantiacus. In: Archives of Biochemistry and Biophysics, 274 (2). pp. 511-517.

PDF pu5rification.pdf - Published Version Restricted to Registered users only Download (1MB) | Request a copy

Abstract

An alpha-D-glucuronidase was purified from the culture filtrates of Thermoascus aurantiacus. A simple colorimetric method for its assay is reported. The enzyme is a single polypeptide chain with a molecular weight of 118,000. It acts optimally at pH 4.5. It shows maximum activity at 65 degrees C. The t 1/2 at 70 degrees C was 40 min. It specifically cleaved the alpha-(1----2) linkage between 4-O-methyl-alpha-D-glucuronic acid and the xylose residue in xylan and several glucurono-xylooligosaccharides.

Item Type:	Journal Article
Publication:	Archives of Biochemistry and Biophysics
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	03 Aug 2010 04:52
Last Modified:	19 Sep 2010 06:12
URI:	http://eprints.iisc.ac.in/id/eprint/30957

Actions (login required)

View Item