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- W2000214304 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 α‐mannosidase and N ‐linked sugars were removed using endo‐β‐ N ‐acetylglucosaminidase F. Analysis ofconformational 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." @default.
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- W2000214304 date "1993-01-25" @default.
- W2000214304 modified "2023-10-15" @default.
- W2000214304 title "Effect of modification of carbohydrate component on properties of glucoamylase" @default.
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- W2000214304 doi "https://doi.org/10.1016/0014-5793(93)81206-f" @default.
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