increased the amount of
released ferulic acid from DSWB more than 14-fold, which is in
accordance with the result obtained for the native UmChlE
(Nieter et al., 2015). In contrast, the reUmChlE was less active on
SBP, even in presence of different pectinase preparations. These
findings are in compliance with the investigations on substrate
specificity of the reUmChlE, where the enzyme was more active
on O-5 ester linked ferulic acid, as present in wheat bran, than
on O-2 or O-6 ester linked ferulic acid found in the pectins of
dicotyledons.