Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region

Fourier transform spectroscopy in the mid-infrared (400-5,000 cm⁻¹) (FT-IR) is being recognized as a powerful tool for analyzing chemical composition of food, with special concern to molecular architecture of food proteins. Unlike other spectroscopic techniques, it provides high-quality spectra with...

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Podrobná bibliografia
Vydané v:	Amino acids Ročník 38; číslo 3; s. 679 - 690
Hlavní autori:	Carbonaro, M, Nucara, A
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	Vienna Vienna : Springer Vienna 01.03.2010 Springer Vienna Springer Nature B.V
Predmet:	Agglomeration Amino acids Analytical Chemistry Animals Biochemical Engineering Biochemistry Biomedical and Life Sciences Chemical composition dietary protein Dietary Proteins Food Food composition Food Technology Foods Fourier transform infrared spectroscopy Fourier transforms Humans Infrared spectroscopy Life Sciences Molecular structure molecular weight Neurobiology Protein Conformation Protein Denaturation Protein interaction Protein Stability Protein structure Protein Structure, Secondary Proteins Proteins - chemistry Proteomics Proteomics - methods Review Article Secondary structure Spectra Spectroscopy Spectroscopy, Fourier Transform Infrared - instrumentation Spectroscopy, Fourier Transform Infrared - methods Spectrum analysis Infrared spectroscopy FT-IR Food proteins Secondary structure
ISSN:	0939-4451, 1438-2199, 1438-2199
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Popis
Shrnutí:	Fourier transform spectroscopy in the mid-infrared (400-5,000 cm⁻¹) (FT-IR) is being recognized as a powerful tool for analyzing chemical composition of food, with special concern to molecular architecture of food proteins. Unlike other spectroscopic techniques, it provides high-quality spectra with very small amount of protein, in various environments irrespective of the molecular mass. The fraction of peptide bonds in α-helical, β-pleated sheet, turns and aperiodic conformations can be accurately estimated by analysis of the amide I band (1,600-1,700 cm⁻¹) in the mid-IR region. In addition, FT-IR measurement of secondary structure highlights the mechanism of protein aggregation and stability, making this technique of strategic importance in the food proteomic field. Examples of applications of FT-IR spectroscopy in the study of structural features of food proteins critical of nutritional and technological performance are discussed.
Bibliografia:	http://dx.doi.org/10.1007/s00726-009-0274-3 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Article-2 ObjectType-Feature-1 content type line 23 ObjectType-Review-3
ISSN:	0939-4451 1438-2199 1438-2199
DOI:	10.1007/s00726-009-0274-3