Hostname: page-component-cd9895bd7-gvvz8 Total loading time: 0 Render date: 2024-12-26T06:02:15.640Z Has data issue: false hasContentIssue false
  • English
  • Français

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
Get access Rights & Permissions [Opens in a new window]

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Chevalier, F, Chobert, J-M, Dalgalarrondo, M, Choiset, Y & Haertlé, T 2002 Maillard glycation of beta-lactoglobulin induces conformation changes. Nahrung 46 58–633.0.CO;2-Y>CrossRefGoogle ScholarPubMed
Esbensen, KH 2001 Multivariate Data Analysis in Practice, 5th edition, Oslo, Norway: CAMO Process ASGoogle Scholar
Guy, PA & Fenaille, F 2006 Contribution of mass spectrometry to assess quality of milk-based products. Mass Spectrometry Reviews 25 290–326CrossRefGoogle ScholarPubMed
Heise, HM 2002 Glucose Measurements by Vibrational Spectroscopy. In Handbook of Vibrational Spectroscopy (Applications of Vibrational Spectroscopy in Life, Pharmaceutical and Natural Sciences) Vol 5, pp. 3280–3294 (Eds Chalmers, JM & Griffiths, PR). Chichester, UK: John Wiley & Sons LtdGoogle Scholar
Kislinger, T 2004 Analysis of protein glycation products by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Current Medicinal Chemistry 11 2185–2193CrossRefGoogle ScholarPubMed
Maillard, L-C 1912 Action des acides amines sur les sucres. Formation des melanoidins par voie methodiqué. Comptes rendus hebdomadaires des séances de l'Académie des Sciences 154 66–68Google Scholar
Morgan, F, Léonil, J, Mollé, D & Bouhallab, S 1999 Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: effect on association behavior and protein conformation. Journal of Agricultural and Food Chemistry 47 83–91CrossRefGoogle Scholar
Oliver, CM, Melton, LD & Stanley, RA 2006a Creating proteins with novel functionality via the Maillard reaction: a review. Critical Reviews in Food Science and Nutrition 46 337–350CrossRefGoogle ScholarPubMed
Oliver, CM, Melton, LD & Stanley, RA 2006b Glycation of caseinate by fructose and fructo-oligosaccharides by controlled heat treatment in the ‘dry’ state. Journal of the Science of Food and Agriculture 86 722–731CrossRefGoogle Scholar
Pereda, M, Aranguren, MI & Marcovich, NE 2007 Characterization of chitosan/caseinate films. Journal of Applied Polymer Science 107 1080–1090CrossRefGoogle Scholar
Sanz, ML, Corzo-Martinez, M, Rastall, RA, Olano, A & Moreno, FJ 2007 Characterization and in vitro digestibility of bovine β-lactoglobulin glycated with galactooligosaccharides. Journal of the Science of Food and Agriculture 55 7916–7925Google Scholar
Steffan, W, Balzer, HH, Lippert, F, Sambor, BC, Bradbury, AGW & Henle, T 2006 Characterization of casein lactosylation by capillary electrophoresis and mass spectrometry. European Food Research and Technology 222 467–471CrossRefGoogle Scholar
Sun, Y, Hayakawa, S & Izumori, K 2004 Modification of ovalbumin with a rare ketohexose through the Maillard reaction: effect on protein structure and gel properties. Journal of Agricultural and Food Chemistry 52 1293–1299CrossRefGoogle ScholarPubMed
Wooster, TJ & Augustin, MA 2007 Rheology of whey protein-dextran conjugate films at the air/water interface. Food Hydrocolloids 21 1072–1080CrossRefGoogle Scholar