Fourier transform raman spectroscopy study of heat-induced gelation of plasma proteins as influenced by pH |
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| Authors: | Dàvila Eduard Parés Dolors Howell Nazlin K |
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| Institution: | Institut de Tecnologia Agroalimentària-CeRTA, Universitat de Girona, Escola Politècnica Superior, Avinguda Lluís Santaló s/n, 17071 Girona, Spain. eduard.davila@udg.es |
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| Abstract: | 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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