| Abstract
| - Fourier transform (FT) Raman spectroscopy was used to elucidate heat-induced structural changesof albumin, globulins, serum, and plasma protein solutions (15% w/w) as affected by pH (4.5, 6.0,and 7.5). Reduction of α-helix and formation of β-sheet, disulfide bond reactions, and exposure andburiedness of hydrophobic groups and amino acid residues were observed. All of these featurescontributed to the formation of strong, irreversible heat-induced gels. The application of a dimensionalityreducing technique such as principal component analysis proved to be useful to determine the mostinfluential qualities of protein samples, as well as the pH-dependent behavior of some of the attributesof both unheated and heated solutions. Analysis of Raman spectra in terms of differencesdemonstrated the interactions of albumin and globulins in co-occurrence and the significant role offibrinogen on the gel's attributes. Keywords: FT-Raman spectroscopy; heat-induced gelation; albumin; globulins; fibrinogen; serum;plasma proteins; principal component analysis
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