Molecular structure and interaction of biopolymers as viewed by Fourier transform infrared spectroscopy: model studies on beta-lactoglobulin

Citation
T. Lefevre et M. Subirade, Molecular structure and interaction of biopolymers as viewed by Fourier transform infrared spectroscopy: model studies on beta-lactoglobulin, FOOD HYDROC, 15(4-6), 2001, pp. 365-376
Citations number
95
Categorie Soggetti
Food Science/Nutrition
Journal title
FOOD HYDROCOLLOIDS
ISSN journal
0268005X → ACNP
Volume
15
Issue
4-6
Year of publication
2001
Pages
365 - 376
Database
ISI
SICI code
0268-005X(200107/11)15:4-6<365:MSAIOB>2.0.ZU;2-K
Abstract
Fourier transform absorption infrared spectroscopy is a powerful and versat ile tool used to determine the molecular structure of biomolecules. This te chnique is now widely used in biochemistry to study the conformation of bio polymers in aqueous solutions and complex systems. However, its enormous po tential in the study of food biopolymers has yet to be reached. The aim of this paper is principally to provide information on biopolymers using Fouri er transform infrared spectroscopy. beta -Lactoglobulin (beta -Lg), the maj or whey protein in the milk of ruminants. is chosen as a model. Emphasis wi ll be put on the different structure levels of proteins in an aqueous solut ion, the protein-protein interactions, and the protein interactions with sm all host-molecules such as phospholipids. (C) 2001 Elsevier Science Ltd. Al l rights reserved.