Molecular flexibility in wheat gluten proteins submitted to heating

FEBS Letters

Hemminga, Marcus A.¹  Popineau, Yves³  Le Meste, Martine²  Hargreaves, Jeremy³ 

[1] Department of Molecular Physics, Wageningen Agricultural University, PO Box 8128, 6700 ET Wageningen, The Netherlands;Département de Physico-Chimie et des Propriétés Sensorielles des Aliments, ENS.BANA, 1 pl. Erasme, CUM, 21000 Dijon, France;Laboratoire de Biochimie et Technologie de Protéines, INRA, BP 1627, 44316 Nantes cedex 03, France

关键词: Prolamin;    Gluten;    ESR;    ST-ESR;    Temperature;    Urea;   

DOI  :  10.1016/0014-5793(95)00825-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Prolamin proteins are responsible for the network that gives wheat dough its viscoelastic properties. Non-prolamin depleted gluten was prepared under conditions that preserve its functionality. Electron Spin Resonance (ESR) was used to provide information about the dynamics of the protein at temperatures between 5 and 90°C by specific spin labelling of its cysteine residues. The spectra were of a composite type, resulting from at least two populations of spin labels largely differing in molecular mobility. The correlation time of the less mobile nitroxide radicals was determined by saturation transfer ESR. Upon heating there was a transfer from the slow to the fast moving population of radicals, and an increase of mobility of this last catagory that followed the Arrhenius law. The effect of temperature on molecular flexibility was reversible. This was not the case for purified, polymerised glutenin subunits extracted from gluten. Urea created similar modifications on gluten as heat.

【 授权许可】

Unknown