Endo-β-N-acetylglucosaminidase (glycopeptide-d-mannosyl-N4-(N-acetyl-d-glucosaminyl)2-asparagine1,4-N-acetyl-β-glucosaminohydrolase, EC 22.214.171.124), homogenized from the culture filtrate of Flavobacterium sp., could liberate about 50% of the sugar chains from the glucoamylase of Rhizopus niveus. The native and carbohydrate-depleted glucoamylases were compared in their various enzymatic properties. It was found that they were identical in their catalytic activities. However, the carbohydrate-depleted glucoamylase was less thermally stable than the native glucoamylase. Moreover, the carbohydrate-depleted glucoamylase was more sensitive to proteinases such as pronase, subtilisin and trypsin. These results suggest that the sugar chains of the glucoamylase contribute to the high stability of the enzyme. However, circular dichroism spectra of the native and carbohydrate-depleted glucoamylase were found to be identical.
|Number of pages
|Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
|Published - Jul 20 1988
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology