Characterization and Exploration of Recombinant Wheat Catalase for Improvement of Wheat-Flour-Processing Quality

The wheat catalase gene ( wcat1) was cloned and overexpressed in Pichia pastoris. The purified wCat1 exhibits its highest activity at pH 7.5 and 35 °C with K_m and V_max of 22.95 mM and 0.24 μmol/min, respectively. wCat1 could markedly improve the farinographic properties of dough, with the stability time increasing and degree of softening decreasing, and enhance the rheological properties of dough. wCat1 could also elevate bread-making quality, with increased specific volume of the bread and decreased hardness, gumminess, and chewiness, which are attributable to increased amounts of SDS-insoluble protein in dough, resulting in extended glutenin networks and thus larger pores in the fermented dough and bread crumb. The decrease of hydrogen peroxide and increase of free thiol groups in wCat1-treated dough suggest that the decomposition of hydrogen peroxide by wCat1 likely promotes disulfide-bond formation and thus the cross-linking of dough proteins.