Variable-temperature Fourier transform infrared spectroscopy can be employed to monitor the denaturation and aggregation of proteins during heat treatment. Information on the changes that occur in protein secondary structure upon heating is provided by detailed examination of the amide I band, as different protein conformations have characteristic amide I frequencies. The objectives of the present study were: (i) to study the changes in protein structure that occur during gelation of whey protein isolate (WPI) and (ii) to correlate the changes in protein structure observed under different physico-chemical conditions to rheological properties of WPI gels prepared under the same conditions. / The FTIR spectra of D2O solutions of WPI at different pHs, ranging from 3 to 10, were recorded as the temperature of the solution was increased from room temperature to 95°C in 5°C increments. In all the solutions studied, the formation of two new bands at 1618--1623 cm -1 and 1678--1684 cm-1 was observed upon heating; these bands are characteristic of aggregate formation and have been previously assigned to antiparallel beta-sheet structure. As the pH increased from 3 to 10, the aggregation temperature of WPI decreased from 85°C to 65°C. / The rheological properties of WPI gels were studied by employing an Instron Universal Testing Machine. The Instron measurements demonstrated that protein concentration, heating temperature, and heating and cooling time are directly related to gel strength. The changes in gel strength as a function of cooling time (for gels prepared by heating at 75°C for 45 min) were correlated to FTIR spectral data for WPI solutions subjected to the same treatment.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.21556 |
| Date | January 1999 |
| Creators | Geara, Charif. |
| Contributors | Ismail, A. A. (advisor) |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Food Science and Agricultural Chemistry.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001657765, proquestno: MQ50774, Theses scanned by UMI/ProQuest. |
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