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 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.
Dàvila
Eduard
E
Institut de Tecnologia Agroalimentària-CeRTA, Universitat de Girona, Escola Politècnica Superior, Avinguda Lluís Santaló s/n, 17071 Girona, Spain. eduard.davila@udg.es
Parés
Dolors
D
Howell
Nazlin K
NK
D001798:Blood Proteins / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry; D005583:Fourier Analysis; D005782:Gels / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D017433:Protein Structure, Secondary; D013059:Spectrum Analysis, Raman
D001798:Blood Proteins; D004220:Disulfides; D005782:Gels