Distribution and location of ethanol soluble proteins (Osborne gliadin) as a function of mixing time in strong wheat flour dough using quantum dots as a labeling tool with confocal laser scanning microscopy


Bozkurt F. , ANSARI S., YAU P., YAZAR G., RYAN V., KOKINI J.

FOOD RESEARCH INTERNATIONAL, vol.66, pp.279-288, 2014 (Journal Indexed in SCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 66
  • Publication Date: 2014
  • Doi Number: 10.1016/j.foodres.2014.09.028
  • Title of Journal : FOOD RESEARCH INTERNATIONAL
  • Page Numbers: pp.279-288
  • Keywords: Gliadin, Quantum dots, Antibody conjugation, Farinograph, Effects of mixing, Confocal laser scanning microscopy, RHEOLOGICAL PROPERTIES, ELECTRON-MICROSCOPY, MOLECULAR-WEIGHT, GLUTEN PROTEINS, FOOD STRUCTURE, BREAD DOUGH, MICROSTRUCTURE, BEHAVIOR, VISUALIZATION, BREADMAKING

Abstract

Gliadin is the more fluid of the two major classes of proteins, gliadins and glutenins, in wheat flour dough and flows best among these two protein classes. Glutenins because of their high elasticity and high hydrophobicity are not likely to disperse as well as gliadins especially if gliadins are not well dispersed or are not present in the dough matrix. The role of native gliadin in this networking process is not well understood and has not been studied by prior researchers due to unavailability of molecular tools to specifically probe gliadin behavior until now. Gliadins contribute to the viscosity and extensibility in dough.