The insertion behaviour of wheat puroindoline-a into diacylgalactosylglycerol films

被引:26
作者
Kooijman, M [1 ]
Orsel, R [1 ]
Hamer, RJ [1 ]
Bekkers, ACAPA [1 ]
机构
[1] TNO, Nutr & Food Res, Dept Cereals & Food Ingredients, NL-3700 AJ Zeist, Netherlands
关键词
puroindoline; protein-lipid interaction; interfacial activity; gas-cell stability; dough;
D O I
10.1006/jcrs.1998.0193
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
In order to study the surface behaviour of puroindoline-a (PIN-a) in the presence of lipid monolayers, protein solutions were injected beneath films of the polar wheat lipid diacylgalactosylglycerol (MGDG). It was found that injection of PIN-a into the sub-phase caused a surface pressure increase of monolayers consisting of MGDG. When PIN-a was injected beneath an MGDG film at an initial surface pressure (pi(initial)) between 9 and 15 mN/m, a relatively fast increase in the surface pressure to 17 +/- 2 mN/m was observed (the maximum surface pressure that could be reached by the protein alone). Then a much more gradual increase in pi was observed. At pi(initial) values exceeding 35 mN/ m, injection of PIN-a resulted in a gradual increase in pi to 49 +/- 1 mN/m, which is equal to the collapse pressure of a pure MGDG monolayer. A gradual increase in the surface pressure was observed after injection of PIN-a beneath an MGDG monolayer with pi(initial) values between 15 and 35 mN/m, but the final value was lower than the collapse pressure of pure MGDG. Injection of peptide-a (a peptide comprising the tryptophan-rich domain of PIN-a) beneath MGDG monolayers also led to a considerable increase in surface pressure. The data are interpreted as insertion of PIN-a or peptide-a into the MGDG films. Tn contrast to this, lipid-transfer protein did not show this behaviour under the same conditions. The present data suggest that PIN-a may be present at the pas-cell surface in dough. However, although the elasticity of mixed PIN-a/MGDG films somewhat decreased owing to protein insertion, the resulting monolayer would still retard disproportionation. (C) 1998 Academic Press.
引用
收藏
页码:43 / 51
页数:9
相关论文
共 14 条
[1]   THE BEHAVIOR OF SOME MODEL PROTEINS AT SOLID LIQUID INTERFACES .1. ADSORPTION FROM SINGLE PROTEIN SOLUTIONS [J].
ARAI, T ;
NORDE, W .
COLLOIDS AND SURFACES, 1990, 51 :1-15
[2]  
Blochet J. E., 1996, BIOCHEMISTRY-US, V25, P12712
[3]   COMPLETE AMINO-ACID-SEQUENCE OF PUROINDOLINE, A NEW BASIC AND CYSTINE-RICH PROTEIN WITH A UNIQUE TRYPTOPHAN-RICH DOMAIN, ISOLATED FROM WHEAT ENDOSPERM BY TRITON X-114 PHASE PARTITIONING [J].
BLOCHET, JE ;
CHEVALIER, C ;
FOREST, E ;
PEBAYPEYROULA, E ;
GAUTIER, MF ;
JOUDRIER, P ;
PEZOLET, M ;
MARION, D .
FEBS LETTERS, 1993, 329 (03) :336-340
[4]   AMINO-ACID-SEQUENCE OF A NONSPECIFIC WHEAT PHOSPHOLIPID TRANSFER PROTEIN AND ITS CONFORMATION AS REVEALED BY INFRARED AND RAMAN-SPECTROSCOPY - ROLE OF DISULFIDE BRIDGES AND PHOSPHOLIPIDS IN THE STABILIZATION OF THE ALPHA-HELIX STRUCTURE [J].
DESORMEAUX, A ;
BLOCHET, JE ;
PEZOLET, M ;
MARION, D .
BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1121 (1-2) :137-152
[5]   GAS CELL STABILIZATION AND GAS RETENTION IN WHEAT BREAD DOUGH [J].
GAN, Z ;
ELLIS, PR ;
SCHOFIELD, JD .
JOURNAL OF CEREAL SCIENCE, 1995, 21 (03) :215-230
[6]  
HUSBAND F, 1995, FOOD MACROMOLECULES, P285
[7]   Competitive adsorption behaviour of wheat flour components and emulsifiers at an air-water interface [J].
Keller, RCA ;
Orsel, R ;
Hamer, RJ .
JOURNAL OF CEREAL SCIENCE, 1997, 25 (02) :175-183
[8]   Spectroscopic characterisation of the lipid-binding properties of wheat puroindolines [J].
Kooijman, M ;
Orsel, R ;
Hessing, M ;
Hamer, RJ ;
Bekkers, ACAPA .
JOURNAL OF CEREAL SCIENCE, 1997, 26 (02) :145-159
[9]  
Lucassen J., 1981, ANIONIC SURFACTANTS, P217
[10]  
MACRITCHIE F, 1973, CEREAL CHEM, V50, P292