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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2010-03

AUTHORS

M. Carbonaro, A. Nucara

ABSTRACT

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 alpha-helical, beta-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. More... »

PAGES

679-690

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00726-009-0274-3

DOI

http://dx.doi.org/10.1007/s00726-009-0274-3

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001299781

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19350368


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