Abstract
Maillard-induced glycosylation of whey protein improves solubility and thermal stability over a wide pH range. However, the relationship between structural changes and functional enhancement upon glycosylation is not well-characterized. Therefore, our objective was to characterise these structural changes and determine the protein conformation at various pH and thermal treatments, using surface-enhanced Raman-spectroscopy. The spectra of glycosylated protein revealed a new peak at 983 cm-1 that can be used as a Raman marker for the early stage glycosylation. Upon glycosylation, structural variations were significant at the disulfide, hydrophobic, amide III, amide II, and amide I regions. Ionisation of carboxyl groups at all tested pH values, and increased β-sheet configuration were also observed. The noted structural modifications imparted molecular rigidity and a consequent resistance to denaturation upon thermal treatment over a wide pH range. These findings can be used to explain various functional enhancements of whey protein upon glycosylation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 313-319 |
| Number of pages | 7 |
| Journal | Food Chemistry |
| Volume | 139 |
| Issue number | 1-4 |
| DOIs | |
| State | Published - Aug 15 2013 |
Bibliographical note
Funding Information:This work was supported by funds from the Midwest Dairy Association TM. We would like to acknowledge Thermo Fisher Scientific (Madison, WI) for the use of the DXR Raman microscope.
Keywords
- Maillard-induced glycosylation
- Structural characterisation
- Surface enhanced Raman spectroscopy (SERS)
- Whey protein