Effects of tyrosinase and laccase on oat proteins and quality parameters of gluten-free oat breads

J Agric Food Chem. 2011 Aug 10;59(15):8385-90. doi: 10.1021/jf200872r. Epub 2011 Jul 18.

Abstract

Effects of a Trichoderma reesei tyrosinase (TYR) and a Trametes hirsuta laccase (LAC) on breadmaking performance of gluten-free oat flour were investigated by SDS-PAGE analysis of oat protein fractions, large deformation rheology, and microscopy of the doughs, as well as on the basis of specific volume and firmness of the gluten-free breads. TYR induced the formation of higher molecular weight proteins in the SDS-PAGE assay. Microscopical analysis showed more intensive protein aggregation in the TYR-treated dough than in the dough without TYR. TYR also increased the firmness of the dough, which was assumed to be because of the cross-linking of oat globulins. LAC did not affect the oat globulins. TYR alone, or together with a commercial Thermomyces lanuginosus xylanase (XYL), increased significantly the specific volume of the gluten-free oat bread. A combination of TYR and XYL also increased the softness of the bread, whereas a combination of LAC and XYL improved the specific volume but did not affect the softness of oat bread. The results thus indicate that cross-linking of oat globulins by TYR, especially with the addition of XYL, was beneficial for improving the texture of gluten-free oat bread.

MeSH terms

  • Avena / chemistry*
  • Bread / analysis*
  • Catalysis
  • Cooking
  • Fungal Proteins / chemistry*
  • Glutens / analysis*
  • Laccase / chemistry*
  • Monophenol Monooxygenase / chemistry*
  • Oxidation-Reduction
  • Plant Proteins / chemistry
  • Trametes / enzymology*
  • Trichoderma / enzymology*

Substances

  • Fungal Proteins
  • Plant Proteins
  • Glutens
  • Laccase
  • Monophenol Monooxygenase