Print Email Facebook Twitter Glycoforms of β-Lactoglobulin with Improved Thermostability and Preserved Structural Packing Title Glycoforms of β-Lactoglobulin with Improved Thermostability and Preserved Structural Packing Author Broersen, K. Voragen, A.G.J. Hamer, R.J. de Jongh, H.H.J. TNO Voeding Publication year 2004 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. Subject NutritionFood technologyβ-LactoglobulinGlycosylationMaillard reactionMonosaccharidesThermal stabilityAminesGlucoseHydrophobicityProteinsThermodynamicsStructural stabilityThermostabilityBiotechnologybeta lactoglobulinamino acid sequenceanalytic methodarticlechemical modificationhydrophobicitynormal distributionprotein secondary structureprotein structureprotein tertiary structurestructure analysisthermostabilityFructoseGlucoseGlycosylationHydrogen-Ion ConcentrationLactoglobulinsMacromolecular SubstancesProtein BindingProtein ConformationProtein DenaturationProtein IsoformsProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryReceptors, FcTemperature To reference this document use: http://resolver.tudelft.nl/uuid:f3060364-6afd-4c0d-9681-f2f9911eb669 DOI https://doi.org/10.1002/bit.20030 TNO identifier 237709 ISSN 0006-3592 Source Biotechnology and Bioengineering, 86 (1), 78-87 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.