Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 54, Issue 20, Pages 7890-7897Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf061512l
Keywords
FT-Raman spectroscopy; heat-induced gelation; albumin; globulins; fibrinogen; serum; plasma proteins; principal component analysis
Funding
- Biotechnology and Biological Sciences Research Council [D18806] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [D18806] Funding Source: Medline
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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 alpha-helix and formation of beta-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.
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