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 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
Subjects
acidity
albumins
alkalinity
Biological and medical sciences
blood proteins
Blood Proteins - chemistry
Disulfides - chemistry
fibrinogen
food chemistry
Food industries
food processing
Fourier Analysis
Fourier transform Raman spectroscopy
Fundamental and applied biological sciences. Psychology
gelation
gels
Gels - chemistry
globulins
heat treatment
Hot Temperature
Hydrogen-Ion Concentration
principal component analysis
protein structure
Protein Structure, Secondary
Raman spectroscopy
Spectrum Analysis, Raman
Temperature
Fourier transformation
plasma proteins
Gelation
globulins
Albumin
Environmental factor
FT-Raman spectroscopy
heat-induced gelation
Globulin
Protein
Heat
Fibrinogen
pH
Serum
Raman spectrometry
Principal component analysis
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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 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
AbstractList 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.
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.
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
Author Dàvila, Eduard
Parés, Dolors
Howell, Nazlin K
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Issue 20
Keywords Temperature
Fourier transformation
plasma proteins
Gelation
globulins
Albumin
Environmental factor
FT-Raman spectroscopy
heat-induced gelation
Globulin
Protein
Heat
Fibrinogen
pH
Serum
Raman spectrometry
Principal component analysis
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Snippet Fourier transform (FT) Raman spectroscopy was used to elucidate heat-induced structural changes of albumin, globulins, serum, and plasma protein solutions (15%...
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SubjectTerms acidity
albumins
alkalinity
Biological and medical sciences
blood proteins
Blood Proteins - chemistry
Disulfides - chemistry
fibrinogen
food chemistry
Food industries
food processing
Fourier Analysis
Fourier transform Raman spectroscopy
Fundamental and applied biological sciences. Psychology
gelation
gels
Gels - chemistry
globulins
heat treatment
Hot Temperature
Hydrogen-Ion Concentration
principal component analysis
protein structure
Protein Structure, Secondary
Raman spectroscopy
Spectrum Analysis, Raman
Title Fourier Transform Raman Spectroscopy Study of Heat-Induced Gelation of Plasma Proteins as Influenced by pH
URI http://dx.doi.org/10.1021/jf061512l
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Volume 54
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