Transglutaminase-Mediated Modification of Glutamine and Lysine Residues in Native Bovine β-Lactoglobulin
| Autor: | Nieuwenhuizen, W.F., Dekker, H.L., Gröneveld, T., Koster, C.G. de, Jong, G.A.H. de |
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| Přispěvatelé: | TNO Voeding |
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
cross linking
Native structure Protein Conformation Glutamine Molecular Sequence Data Lactoglobulins Circular dichroism β-lactoglobulin Food technology Protein Structure Secondary Bovinae protein modification beta lactoglobulin Streptoverticillium surface tension Animals Amino Acid Sequence Reaction kinetics Nutrition Streptomyces mobaraensis Crosslinking lysine nonhuman Binding Sites Transglutaminases Mass spectrometry article Proteins matrix assisted laser desorption ionization time of flight mass spectrometry Transglutaminase Streptomyces protein glutamine gamma glutamyltransferase Milk Nondenaturing conditions Amino Acid Substitution Cattle protein secondary structure deamination Chemical modification Biotechnology Protein Binding |
| Zdroj: | Biotechnology and Bioengineering, 3, 85, 248-258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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