Found 1 publication. Displayed publication 1
Expand all publications       Show all as text (SweetDB notation)
1. (Article ID: 6614)
 
Neustroev KN, Golubev AM, Firsov LM, Ibatullin FM, Protasevich II, Makarov AA
Effect of modification of carbohydrate component on properties of glucoamylase
FEBS Letters 316 (1993) 157-160
 

In this study, we investigated enzymatic deglycosylation of glucoamylase from Aspergillus awamori X 100/D27, a glycoprotein which has two N-linked and about forty short mannose-bearing O-linked sugars per molecule. O-Linked sugars were modified by treatment with α-mannosidase and N-linked sugars were removed using endo-β-N-acetylglucosaminidase F. Analysis of conformational changes following deglycosylation suggests that O-linked sugars essentially contribute to the stabilization of glucoamylase domains. Modification of the carbohydrate component by adding 1-deoxymannojirimycin to the culture medium induced inhibition of α-mannosidases involved in the processing, leading to a more complete glycosylation and, consequently, to a higher stability of the enzyme.

The publication contains the following compound(s):
 

Expand this publication

Resort publications by:

New query Export IDs Home Help

Execution: <1 sec