NDLI: Purification And Characterization Of An Alpha-D-glucuronidase From A Thermophilic Fungus, Thermoascus Aurantiacus

Content Provider	Indian Institute of Science (IISc)
Author	Khandke, Kiran M. Vithayathil, P. J. Murthy, S. K.
Copyright Year	1989
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.
File Format	PDF
Journal	PeerReviewed
Language	English
Publisher	Elsevier Science
Publisher Date	1989-11-01
Access Restriction	Authorized
Subject Keyword	Biochemistry
Content Type	Text
Resource Type	Article

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