Tyrosine cross-links: molecular basis of gluten structure and function

J Agric Food Chem. 2001 May;49(5):2627-32. doi: 10.1021/jf010113h.


The formation of the large protein structure known as "gluten" during dough-mixing and bread-making processes is extremely complex. It has been established that a specific subset of the proteins comprising gluten, the glutenin subunits, directly affects dough formation and breadmaking quality. Glutenin subunits have no definitive structural differences that can be directly correlated to their ability to form gluten and affect dough formation or breadmaking quality. Many protein structural studies, as well as mixing and baking studies, have postulated that disulfide bonds are present in the gluten structure and contribute to the process of dough formation through the process of disulfide-sulfhydryl exchange. Evidence presented here indicates that tyrosine bonds form in wheat doughs during the processes of mixing and baking, contributing to the structure of the gluten network. The relative contributions of tyrosine bonds and disulfide--sulfhydryl interchange are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Bread
  • Chromatography, High Pressure Liquid
  • Cooking
  • Disulfides
  • Glutens / analysis*
  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Sulfhydryl Compounds
  • Triticum / chemistry
  • Tyrosine / analysis*


  • Amino Acids
  • Disulfides
  • Sulfhydryl Compounds
  • Tyrosine
  • Glutens