Commercial food proteins were used in order to study the relationship between hydrophobicity and two functional properties: emulsification and foaming. Hydrophobicity determined by sodium dodecyl sulfate (SDS) binding method and the cis-parinaric acid (CPA) fluorescence probe method gave poor statistical correlation with foaming and emulsification. The SDS binding method gave higher hydrophobicity and higher correlation values with foaming and emulsifying, than the fluorescence probe CPA method. / Fourier Transform Infrared (FTIR) spectroscopy was used to study the secondary structures, of the commercial food proteins. Infrared spectra of the protein samples with or without denaturing agents (SDS, urea, and guanidine) in the region of the amide I and II bands were determined in deuterium oxide (D$ sb{2}$O) buffer. Fourier self-deconvolution was used to study infrared band positions. BSA was an $ alpha$-helix protein, and in the presence of SDS, due to protein unfolding, exhibited a random coil structure. By correlating their infrared spectra to predetermined peak positions in the protein samples, it was shown that the legume proteins contained $ beta$-structure, and as SDS was added, exhibited non-ordered structures. The spectra of gluten samples were obtained only in the presence of SDS, showing either random coil, or non-ordered structures.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.69580 |
| Date | January 1993 |
| Creators | Arbabzadeh, Sima-Dokht |
| Contributors | Alli, I. (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: 001338373, proquestno: AAIMM87922, Theses scanned by UMI/ProQuest. |
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