Print Email Facebook Twitter Transglutaminase-Mediated Modification of Glutamine and Lysine Residues in Native Bovine β-Lactoglobulin Title Transglutaminase-Mediated Modification of Glutamine and Lysine Residues in Native Bovine β-Lactoglobulin Author Nieuwenhuizen, W.F. Dekker, H.L. Gröneveld, T. de Koster, C.G. de Jong, G.A.H. TNO Voeding Publication year 2004 Abstract Bovine β-lactoglobulin (BLG) is a major component in whey and its physical properties are important for the texture of many dairy-based foods. Modification of proteins with transglutaminase from Streptoverticillium mobaraense (MTGase) can be used to alter their physical properties. MTGase-mediated modification of native BLG was until now, however, not effective. Here we report a method that allows for the enzymatic modification of native BLG with MTGase. Lysines 8, 77, and 141 were modified with α-N-carbobenzyloxy-glutamine-glycine and glutamines 35, 59, 68, and 155 were modified with 6-aminohexanoic acid under nonreducing and nondenaturing conditions. MTGase-mediated BLG crosslinking is hampered by the low reactivity of the lysines and enzymatic deamidation of the glutamines prevails. Modification of BLG with poly-lysine yields a BLG derivative with increased affinity for the water-air interface and stronger surface tension lowering capacities than normal BLG. Hence, this modification method offers the opportunity to change the functional properties of BLG and to prepare novel protein foods. © 2004 Wiley Periodicals, Inc. Subject NutritionFood technologyβ-lactoglobulinCircular dichroismMass spectrometryNative structureProtein modificationTransglutaminaseChemical modificationCrosslinkingProteinsReaction kineticsSurface tensionNondenaturing conditionsBiotechnologybeta lactoglobulinglutaminelysineprotein glutamine gamma glutamyltransferasearticlecircular dichroismcross linkingdeaminationmatrix assisted laser desorption ionization time of flight mass spectrometrynonhumanprotein modificationprotein secondary structureStreptoverticilliumsurface tensionAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCattleGlutamineLactoglobulinsLysineMilkMolecular Sequence DataProtein BindingProtein ConformationProtein Structure, SecondaryStreptomycesSurface TensionTransglutaminasesBovinaeStreptomycesStreptomyces mobaraensis To reference this document use: http://resolver.tudelft.nl/uuid:4494be24-94cf-4fb5-a69e-43032d36cb10 DOI https://doi.org/10.1002/bit.10898 TNO identifier 237617 ISSN 0006-3592 Source Biotechnology and Bioengineering, 85 (3), 248-258 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.