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Use of FTIR and mass spectrometry for characterization of glycated caseins

Published online by Cambridge University Press:  05 January 2009

Christine M Oliver ,
Ashwini Kher ,
Don McNaughton  and
Mary Ann Augustin
Christine M Oliver*
Affiliation:
School of Chemistry, Monash University, Clayton, VIC 3800, Australia
Ashwini Kher
Affiliation:
School of Chemistry, Monash University, Clayton, VIC 3800, Australia
Don McNaughton
Affiliation:
School of Chemistry, Monash University, Clayton, VIC 3800, Australia
Mary Ann Augustin
Affiliation:
School of Chemistry, Monash University, Clayton, VIC 3800, Australia Food Science Australia, 671 Sneydes Road, Werribee, VIC 3030, Australia CSIRO Food Futures Flagship
*
*For correspondence; e-mail: Christine1.Oliver@csiro.au or ollieincork@yahoo.co.nz
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Abstract

This study investigates the potential of Fourier transform infrared spectroscopy (FTIR) to monitor glycation-induced changes in protein structure. Aqueous solutions of sodium caseinate and glucose (1:2 w/w, pH 6·7) were heated at 90°C for 0, 10, 20, 40 and 60 min. Evidence for caseinate glycation was obtained by mass spectrometry techniques (electrospray (ESI) and matrix-assisted laser desorption ionisation (MALDI)). FTIR was able to discriminate between glycated and non-glycated sodium caseinate, when the data were analysed by multivariate statistical methods; principal component analysis (PCA) and soft independent modelling of class analogy (SIMCA). The techniques used were complementary and provided different levels of information about the glycated samples.

Keywords

GlycationMaillardcaseinmass spectrometryFourier transform infrared spectroscopy
Type
Research Article
Information
Journal of Dairy Research , Volume 76 , Issue 1 , February 2009 , pp. 105 - 110
Copyright
Copyright © Proprietors of Journal of Dairy Research 2009

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