Abstract:
: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 alpha-mannosidase and N-linked sugars were removed using endo-beta-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 alpha-mannosidases involved in the processing, leading to a more complete glycosylation and, consequently, to a higher stability of the enzyme.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Neustroev KN,Golubev AM,Firsov LM,Ibatullin FM,Protasevich II,Makarov AAdoi
10.1016/0014-5793(93)81206-fsubject
Has Abstractpub_date
1993-01-25 00:00:00pages
157-60issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(93)81206-Fjournal_volume
316pub_type
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