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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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|
|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|
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