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

K M Khandke; P J Vithayathil; S K Murthy

doi:10.1016/0003-9861(89)90464-5

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

Arch Biochem Biophys. 1989 Nov 1;274(2):511-7. doi: 10.1016/0003-9861(89)90464-5.

Authors

K M Khandke¹, P J Vithayathil, S K Murthy

Affiliation

¹ Department of Biochemistry, Indian Institute of Science, Bangalore.

PMID: 2802623
DOI: 10.1016/0003-9861(89)90464-5

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Ascomycota / enzymology*
Enzyme Activation
Enzyme Stability
Fungal Proteins / isolation & purification*
Glucuronidase / isolation & purification*
Glucuronidase / metabolism
Hot Temperature
Hydrolysis
Substrate Specificity

Substances

Fungal Proteins
Glucuronidase