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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Published in | Journal of agricultural and food chemistry Vol. 54; no. 20; pp. 7890 - 7897 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
04.10.2006
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Subjects | |
Online Access | Get full text |
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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 |
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Bibliography: | http://dx.doi.org/10.1021/jf061512l ark:/67375/TPS-NKQHF9KM-7 istex:D1E514349A39470DEE6B6194F8B85FD9DAC2A650 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-8561 1520-5118 |
DOI: | 10.1021/jf061512l |