Glycation Reactions of Casein Micelles
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
After suspensions of micellar casein or nonmicellar sodium caseinate had been heated, respectively, in the presence and absence of glucose for 0-4 h at 100 degrees C, glycation compounds were quantitated. The formation of Amadori products as indicators for the "early" Maillard reaction were in the same range for both micellar and nonmicellar caseins, indicating that reactive amino acid side chains within the micelles are accessible for glucose in a comparable way as in nonmicellar casein. Significant differences, however, were observed concerning the formation of the advanced glycation end products (AGEs), namely, N-epsilon-carboxymethyllysine (CML), pyrraline, pentosidine, and glyoxal-lysine dimer (GOLD). CML could be observerd in higher amounts in nonmicellar casein, whereas in the micelles the pyrraline formation was increased. Pentosidine and GOLD were formed in comparable amounts. Furthermore, the extent of protein cross-linking was significantly higher in the glycated casein micelles than in the nonmicellar casein samples. Dynamic light scattering and scanning electron microscopy showed that glycation has no influence on the size of the casein micelles, indicating that cross-linking occurs only in the interior of the micelles, but altered the surface morphology. Studies on glycation and nonenzymatic cross-linking can contribute to the understanding of the structure of casein micelles.
Details
Original language | English |
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Pages (from-to) | 2953-2961 |
Number of pages | 9 |
Journal | Journal of Agricultural and Food Chemistry |
Volume | 64 |
Issue number | 14 |
Publication status | Published - 13 Apr 2016 |
Peer-reviewed | Yes |
External IDs
Scopus | 84964680295 |
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WOS | 000374275100018 |
researchoutputwizard | legacy.publication#74699 |
ORCID | /0000-0002-2391-6025/work/142250172 |
Keywords
Keywords
- casein micelle, sodium caseinate, glycation, Maillard reaction, cross-link, scanning electron microscopy, SCANNING-ELECTRON-MICROSCOPY, HEAT-TREATED MILK, MAILLARD-REACTION, BETA-CASEIN, PROTEIN GLYCATION, MODEL SYSTEMS, CROSS-LINKING, AMINO-ACID, LYSINE, PRODUCTS