Purification and characterization of an alpha-D-glucuronidase from a thermophilic fungus, Thermoascus aurantiacus.
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.
Khandke
K M
KM
Department of Biochemistry, Indian Institute of Science, Bangalore.
Vithayathil
P J
PJ
Murthy
S K
SK
D001203:Ascomycota / Q000201:enzymology*; D004789:Enzyme Activation; D004795:Enzyme Stability; D005656:Fungal Proteins / Q000302:isolation & purification*; D005966:Glucuronidase / Q000302:isolation & purification* / Q000378:metabolism; D006358:Hot Temperature; D006868:Hydrolysis; D013379:Substrate Specificity
D005656:Fungal Proteins; D005966:Glucuronidase