Veratiyl alcohol

Effect of Veratiyl Alcohol. At pH 5.0 the purified lignin peroxidase was not inactivated under the conditions tested. At pH 3.0 the enzyme lost its activity when incubated at 20°C for 38 days, and the presence of veratryl alcohol could not stabilize it. 100 mM veratryl alcohol even inactivated the enzyme to some extent. Ionic strength did not significantly affect the activities. The effect of veratryl alcohol was the same when unfractionated enzyme was used. This time the ionic strength in the activity assay mixture affected the activities, probably because one enzyme in the unfractionated preparation is sensitive to high ionic strength 12),... 

Culture media partially optimized for P. chrysosporium (50) unless otherwise indicated, nmol/min. measured at room temperature per mg dry mycelial weight for vanillylacetoneas a Mn -dependent peroxidase substrate and veratiyl alcohol as a lignin peroxidase substrate 0 denotes activity below detectable limit while — indicates assay not performed. Time, at 39 C for P. chrysosporium or at 30 C for L edodes, after inoculation when maximum activity appears (d ). Interval over which C02 evolution from dehydrogenative polymerizate (DHP) of [ring- /- C]conifeiyl alcohol is measured (days after inoculation). Culture media partially optimized for L. edodes at 22 C (83). 

---