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.

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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 °C. The t1/2 at 70 °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:	14 Feb 2008
Last Modified:	19 Sep 2010 04:42
URI:	http://eprints.iisc.ac.in/id/eprint/12790

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