1H NMR relaxation studies of protein-polysaccharide mixtures

被引:23
作者
Ducel, V. [1 ,3 ]
Pouliquen, D. [2 ]
Richard, J. [3 ]
Boury, F. [1 ]
机构
[1] INSERM, U646, F-49100 Angers, France
[2] Inst Biol, INSERM, U601, F-44735 Nantes, France
[3] Ethypharm, F-92213 St Cloud, France
关键词
Proton NMR relaxation; Rotational and translational motion; Protein-polysaccharide interactions;
D O I
10.1016/j.ijbiomac.2008.07.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
NMR water proton relaxation was used to characterize the structure of plant proteins and plant protein-polysaccharide mixtures in aqueous solutions. The method is based on the mobility determination of the water molecules in the biopolymer environment in solutions through relaxation time measurements. Differences of conformation between pea globulin and alpha gliadin seem to control the water molecules mobility in their environment. As deduced from the study of complexes, the electrostatic interactions may also play a major role in the water molecule motions. The phase separation induced under specific conditions seems to promote the translational diffusion of structured water molecules whereas the rotational motion was more restricted. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:359 / 366
页数:8
相关论文
共 46 条
[1]   Complexation mechanism of bovine serum albumin and poly(allylamine hydrochloride) [J].
Ball, V ;
Winterhalter, M ;
Schwinte, P ;
Lavalle, P ;
Voegel, JC ;
Schaaf, P .
JOURNAL OF PHYSICAL CHEMISTRY B, 2002, 106 (09) :2357-2364
[2]   Interactions of potato starch with selected polysaccharide hydrocolloids as measured by low-field NMR [J].
Baranowska, Hanna M. ;
Sikora, M. ;
Kowalski, S. ;
Tornasik, P. .
FOOD HYDROCOLLOIDS, 2008, 22 (02) :336-345
[3]   NMR and FTIR studies of hydrated pea proteins [J].
Belton, PS ;
Bogracheva, T ;
Cserhalmi, Z ;
Czukor, B ;
Grant, A ;
Lambert, N ;
Wellner, N .
FOOD HYDROCOLLOIDS, 1997, 11 (04) :485-491
[4]   H-1-NMR RELAXATION-TIME STUDIES OF THE HYDRATION OF THE BARLEY PROTEIN-C-HORDEIN [J].
BELTON, PS ;
GIL, AM ;
TATHAM, A .
JOURNAL OF THE CHEMICAL SOCIETY-FARADAY TRANSACTIONS, 1994, 90 (08) :1099-1103
[5]   Proton and carbon NMR measurements of the effects of hydration on the wheat protein ω-gliadin [J].
Belton, PS ;
Gil, AM ;
Grant, A ;
Alberti, E ;
Tatham, AS .
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY, 1998, 54 (07) :955-966
[6]   New insight into the solution structures of wheat gluten proteins from Raman optical activity [J].
Blanch, EW ;
Kasarda, DD ;
Hecht, L ;
Nielsen, K ;
Barron, LD .
BIOCHEMISTRY, 2003, 42 (19) :5665-5673
[7]   13C and 1H solid state NMR investigation of hydration effects on gluten dynamics [J].
Calucci, L ;
Forte, C ;
Galleschi, L ;
Geppi, M ;
Ghiringhelli, S .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2003, 32 (3-5) :179-189
[8]   Monte Carlo simulations of polyelectrolyte-protein complexation [J].
Carlsson, F ;
Linse, P ;
Malmsten, M .
JOURNAL OF PHYSICAL CHEMISTRY B, 2001, 105 (38) :9040-9049
[9]   THE CONFORMATIONAL STRUCTURE OF A-GLIADIN - INTRINSIC VISCOSITIES UNDER CONDITIONS APPROACHING THE NATIVE-STATE AND UNDER DENATURING CONDITIONS [J].
COLE, EW ;
KASARDA, DD ;
LAFIANDRA, D .
BIOCHIMICA ET BIOPHYSICA ACTA, 1984, 787 (03) :244-251
[10]  
Crevieu I, 1996, NAHRUNG, V40, P237, DOI 10.1002/food.19960400502