Fourier Transform Raman Spectroscopy Study of Heat-Induced Gelation of Plasma Proteins as Influenced by pH

Fourier transform (FT) Raman spectroscopy was used to elucidate heat-induced structural changes of 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 and buried...

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Bibliographic Details
Published inJournal of agricultural and food chemistry Vol. 54; no. 20; pp. 7890 - 7897
Main Authors Dàvila, Eduard, Parés, Dolors, Howell, Nazlin K
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 04.10.2006
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Summary:Fourier transform (FT) Raman spectroscopy was used to elucidate heat-induced structural changes of 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 and buriedness of hydrophobic groups and amino acid residues were observed. All of these features contributed to the formation of strong, irreversible heat-induced gels. The application of a dimensionality reducing technique such as principal component analysis proved to be useful to determine the most influential qualities of protein samples, as well as the pH-dependent behavior of some of the attributes of both unheated and heated solutions. Analysis of Raman spectra in terms of differences demonstrated the interactions of albumin and globulins in co-occurrence and the significant role of fibrinogen on the gel's attributes. Keywords: FT-Raman spectroscopy; heat-induced gelation; albumin; globulins; fibrinogen; serum; plasma proteins; principal component analysis
Bibliography:http://dx.doi.org/10.1021/jf061512l
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ISSN:0021-8561
1520-5118
DOI:10.1021/jf061512l