Characterising protein, salt and water interactions with combined vibrational spectroscopic techniques.

Abstract:

:In this paper a combination of NIR spectroscopy and FTIR and Raman microspectroscopy was used to elucidate the effects of different salts (NaCl, KCl and MgSO(4)) on structural proteins and their hydration in muscle tissue. Multivariate multi-block technique Consensus Principal Component Analysis enabled integration of different vibrational spectroscopic techniques: macroscopic information obtained by NIR spectroscopy is directly related to microscopic information obtained by FTIR and Raman microspectroscopy. Changes in protein secondary structure observed at different concentrations of salts were linked to changes in protein hydration affinity. The evidence for this was given by connecting the underlying FTIR bands of the amide I region (1700-1600 cm(-1)) and the water region (3500-3000 cm(-1)) with water vibrations obtained by NIR spectroscopy. In addition, Raman microspectroscopy demonstrated that different cations affected structures of aromatic amino acid residues differently, which indicates that cation-π interactions play an important role in determination of the final structure of protein molecules.

journal_name

Food Chem

journal_title

Food chemistry

authors

Perisic N,Afseth NK,Ofstad R,Hassani S,Kohler A

doi

10.1016/j.foodchem.2012.10.117

subject

Has Abstract

pub_date

2013-05-01 00:00:00

pages

679-86

issue

1

eissn

0308-8146

issn

1873-7072

pii

S0308-8146(12)01691-3

journal_volume

138

pub_type

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