Effect of modification of carbohydrate component on properties of glucoamylase

FEBS Letters

Ibatullin, F.M.²  Neustroev, K.N.²  Makarov, A.A.¹  Golubev, A.M.²  Firsov, L.M.²  Protasevich, I.I.¹ 

[1] Institute of Molecular Biology, Moscow, Russian Federation;Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation

关键词: Glucoamylase;    Glycoprotein;    Deglycosylation;   

DOI  :  10.1016/0014-5793(93)81206-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown