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Molecular structure and interaction of biopolymers as viewed by Fourier transform infrared spectroscopy model studies on β-lactoglobulin.pdf
Food Hydrocolloids 15 (2001) 365±376
/locate/foodhyd
Molecular structure and interaction of biopolymers as viewed by Fourier transform infrared spectroscopy: model studies on b-lactoglobulin
Thierry Lefeávre, Muriel Subirade*
Universite? Laval, Faculte? des sciences de lagriculture et de lalimentation, Centre de recherches en Sciences et Technologie du Lait (STELA), Pavillon Paul Comtois, Sainte-Foy, Que?bec, Canada G1K 7P4
Received 21 September 2000; accepted 28 March 2001
Abstract
Fourier transform absorption infrared spectroscopy is a powerful and versatile tool used to determine the molecular structure of biomolecules. This technique is now widely used in biochemistry to study the conformation of biopolymers in aqueous solutions and complex systems. However, its enormous potential in the study of food biopolymers has yet to be reached. The aim of this paper is principally to provide information on biopolymers using Fourier transform infrared spectroscopy. b-Lactoglobulin (b-Lg), the major whey protein in the milk of ruminants, is chosen as a model. Emphasis will be put on the different structure levels of proteins in an aqueous solution, the protein± protein interactions, and the protein interactions with small host-molecules such as phospholipids. q 2001 Elsevier Science Ltd. All rights reserved.
Keywords: Biopolymer; Molecular structure; Functional properties; Interaction; FTIR spectroscopy
1. Introduction
The structure of biomolecules is the main factor that determines their biological function. Among biomolecules, some biopolymers, especially proteins, are technologically important due to their texturing, hydrating, and interfacial stabilizing capacities. These techno-functional properties are also directly related to their molecular structure. Thus, basic structural knowledge of biopolymers is an important step towards understanding their functional properties. Reaching this goal is made dif?cult by the strong inˉuence of medium conditions (pH, presence of
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