Principal component similarity analysis of Raman spectra to study the effects of pH,heating, and kappa-carrageenan on whey protein structure |
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Authors: | Alizadeh-Pasdar Nooshin Nakai Shuryo Li-Chan Eunice C Y |
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Institution: | Faculty of Agricultural Sciences, Food, Nutrition, and Health, Food Science Building, The University of British Columbia, 6640 N.W. Marine Drive, Vancouver, British Columbia, Canada V6T 1Z4. |
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Abstract: | Raman spectroscopy was used to elucidate structural changes of beta-lactoglobulin (BLG), whey protein isolate (WPI), and bovine serum albumin (BSA), at 15% concentration, as a function of pH (5.0, 7.0, and 9.0), heating (80 degrees C, 30 min), and presence of 0.24% kappa-carrageenan. Three data-processing techniques were used to assist in identifying significant changes in Raman spectral data. Analysis of variance showed that of 12 characteristics examined in the Raman spectra, only a few were significantly affected by pH, heating, kappa-carrageenan, and their interactions. These included amide I (1658 cm(-1)) for WPI and BLG, alpha-helix for BLG and BSA, beta-sheet for BSA, CH stretching (2880 cm(-1)) for BLG and BSA, and CH stretching (2930 cm(-1)) for BSA. Principal component analysis reduced dimensionality of the characteristics. Heating and its interaction with kappa-carrageenan were identified as the most influential in overall structure of the whey proteins, using principal component similarity analysis. |
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