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Transglutaminase-Mediated Modification of Glutamine and Lysine Residues in Native Bovine β-Lactoglobulin

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Author: Nieuwenhuizen, W.F. · Dekker, H.L. · Gröneveld, T. · Koster, C.G. de · Jong, G.A.H. de
Institution: TNO Voeding
Source:Biotechnology and Bioengineering, 3, 85, 248-258
Identifier: 237617
doi: doi:10.1002/bit.10898
Keywords: Nutrition · Food technology · β-lactoglobulin · Circular dichroism · Mass spectrometry · Native structure · Protein modification · Transglutaminase · Chemical modification · Crosslinking · Proteins · Reaction kinetics · Surface tension · Nondenaturing conditions · Biotechnology · beta lactoglobulin · glutamine · lysine · protein glutamine gamma glutamyltransferase · article · circular dichroism · cross linking · deamination · matrix assisted laser desorption ionization time of flight mass spectrometry · nonhuman · protein modification · protein secondary structure · Streptoverticillium · surface tension · Amino Acid Sequence · Amino Acid Substitution · Animals · Binding Sites · Cattle · Glutamine · Lactoglobulins · Lysine · Milk · Molecular Sequence Data · Protein Binding · Protein Conformation · Protein Structure, Secondary · Streptomyces · Surface Tension · Transglutaminases · Bovinae · Streptomyces · Streptomyces mobaraensis


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.