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Glycoforms of β‐lactoglobulin with improved thermostability and preserved structural packing
Author(s) -
Broersen Kerensa,
Voragen Alphons G. J.,
Hamer Rob J.,
de Jongh Harmen H. J.
Publication year - 2004
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.20030
Subject(s) - thermostability , chemistry , glycosylation , fructose , glycoprotein , thermal stability , primary (astronomy) , biochemistry , chromatography , protein tertiary structure , protein engineering , chemical modification , protein folding , protein quaternary structure , organic chemistry , enzyme , protein subunit , physics , astronomy , gene
In this article we show how various degrees of glycosylation can be used to control the thermal stability of proteins. The primary amines of β‐lactoglobulin were glycosylated with glucose or fructose within a range of non‐denaturing reaction parameters. The modified fractions were characterized and analyzed for structural stability and hydrophobic exposure. The modification procedure gave rise to the production of glycoproteins with a well‐defined Gaussian distribution, where glucose appeared more reactive than fructose. The integrity of the secondary, tertiary, and quaternary structures remained unaffected by the modification procedure. However, upon heating the stability of the modified fractions increased up to 6 K. Here we demonstrate the effects on the thermodynamic properties of proteins by glycosylation; this work serves as a first step in understanding and controlling the process underlying aggregation of glycosylated proteins. © 2004 Wiley Periodicals, Inc.