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
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
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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