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• W2159314580 endingPage "1713" @default.
• W2159314580 startingPage "1707" @default.
• W2159314580 abstract "In this study, we use FTIR spectroscopy to probe the conformational changes of beta-lactoglobulin (beta-LG)-the main constituent of whey proteins-as subjected to enzymatic cross-linking by transglutaminase. We investigate both the amide I region (1600-1700 cm(-1)) and the C-H stretching region (2800-3100 cm(-1)). In the amide I region, spectra of denatured conformations of beta-LG, known to be necessary for cross-linking, differ according to the denaturation procedure, i.e., chemical or thermal treatment. Denaturation by chemical denaturants, dithiothreitol (DTT) or beta-mercaptoethanol, show no effect on the alpha-helix, while shifting the monomer dimer equilibrium toward higher monomer concentration. On the other hand, denaturing by thermal treatment dissociates the beta-sheets in the native structure, leading to new intermolecular beta-sheets being formed. Preheated then enzyme cross-linked beta-LG molecules show very similar spectra in the amide I region to the molecules with no cross-linking, indicating minimal effects of the cross-links on the carbonyl stretching mode. However, chemically denatured (using beta-mercaptoethanol) then enzyme cross-linked beta-LG molecules show noticeable diminution in the alpha-helix band and formation of strong hydrogen-bonded intermolecular beta-sheets. In the C-H stretching region, preheated then enzyme cross-linked beta-LG molecules exhibit a different degree of exposure of aliphatic amino acids due to the enzyme action. The same behavior is observed for DTT-treated then enzyme cross-linked beta-LG molecules. Generally, the changes in the C-H stretching region clearly indicate that hydrophobic interactions are altered upon enzymatic cross-linking." @default.
• W2159314580 created "2016-06-24" @default.
• W2159314580 creator A5002020272 @default.
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• W2159314580 date "2006-05-24" @default.
• W2159314580 modified "2023-09-25" @default.
• W2159314580 title "Enzymatic Cross-Linking of β-Lactoglobulin: Conformational Properties Using FTIR Spectroscopy" @default.
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• W2159314580 doi "https://doi.org/10.1021/bm050928p" @default.
• W2159314580 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16768388" @default.
• W2159314580 hasPublicationYear "2006" @default.
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