A. Silva et al., OCTYL GLUCOSIDE INHIBITS [C-14] DHP MINERALIZATION WHEREAS PEROXIDASE-ACTIVITY IS STIMULATED IN PHANEROCHAETE-CHRYSOSPORIUM, Applied biochemistry and biotechnology, 60(1), 1996, pp. 83-94
Octyl glucoside stimulated peroxidase formation in Phanerochaete chrys
osporium ME-446 cultivated in cellulose-based media. Addition of 0.1%
of the nonionic surfactant resulted in a ninefold (143 U/L) and sixfol
d (119 U/L) increase in LiP formation under conditions of N limitation
and N excess, respectively. Octyl glucoside also stimulated MnP forma
tion, but to a lesser extent than observed with LiP. The cellobiose-ox
idizing enzymes (cellobiose dehydrogenase and cellobiose:quinone oxido
reductase) were stimulated by octyl glucoside when used at a concentra
tion of up to 0.05%, but higher concentrations gave values similar to
those for the controls. Little proteolytic activity was detected in th
e presence of the surfactant. In general, activities of the enzymes st
udied were of the same order as those seen using Tween-80. In contrast
with Tween-80, octyl glucoside markedly inhibited [C-14]DHP mineraliz
ation. Attempts to account for the observed inhibition of synthetic li
gnin degradation by P. chrysosporium in the presence of octyl glucosid
e are discussed.