Enzymatic modifications of gluten protein: Oxidative enzymes

Abstract

Oxidative enzymes treat weak flours in order to restore the gluten network of damaged wheat flour and reduce the economic and technological losses. The present review concentrates on oxidative exogenous enzymes (transglutaminase, laccase, glucose oxidase, hexose oxidase) and oxidative endogenous enzymes (tyrosinase, peroxidase, catalase, sulfhydryl oxidase, lipoxygenase, lipase, protein disulfide isomerase, NAD(P)H-dependent dehydrogenase, thioredoxin reductase and glutathione reductase) and their effects on the rheological, functional, and conformational features of gluten and its subunits. Overall, transglutaminase is used in wheat-based foods through introducing isopeptide bonds (ε-γ glutamyl-lysine). Glucose oxidase, hexose oxidase, peroxidase, sulfhydryl oxidase, lipase, and lipoxygenase form disulfide and nondisulfide bonds through producing hydrogen peroxide. Laccase, tyrosinase, and protein disulfide isomerase form cross-links between tyrosine and cysteine residues by generating radicals. Thioredoxin reductase and glutathione reductase create new inter disulfide bonds. The effect of oxidative enzymes on the formation of covalent cross-linkages were substantially more than non-covalent bonds in gluten structure.

Keywords: Enzymatic modification; Gluten; Oxidative enzymes; Physicochemical properties; Rheological properties.