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.