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Glycoforms of β-Lactoglobulin with Improved Thermostability and Preserved Structural Packing

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Author: Broersen, K. · Voragen, A.G.J. · Hamer, R.J. · Jongh, H.H.J. de
Type:article
Date:2004
Institution: TNO Voeding
Source:Biotechnology and Bioengineering, 1, 86, 78-87
Identifier: 237709
doi: doi:10.1002/bit.20030
Keywords: Nutrition · Food technology · β-Lactoglobulin · Glycosylation · Maillard reaction · Monosaccharides · Thermal stability · Amines · Glucose · Hydrophobicity · Proteins · Thermodynamics · Structural stability · Thermostability · Biotechnology · beta lactoglobulin · amino acid sequence · analytic method · article · chemical modification · hydrophobicity · normal distribution · protein secondary structure · protein structure · protein tertiary structure · structure analysis · thermostability · Fructose · Glucose · Glycosylation · Hydrogen-Ion Concentration · Lactoglobulins · Macromolecular Substances · Protein Binding · Protein Conformation · Protein Denaturation · Protein Isoforms · Protein Structure, Quaternary · Protein Structure, Secondary · Protein Structure, Tertiary · Receptors, Fc · Temperature

Abstract

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.