Twenty-six fungal cultures, including ten (= ) cultures and five other capnodiaceous fungi, were examined for extracellular chloroperoxidase production on four growth media. Only the cultures produced enzyme activity and enzyme production was highest on growth in a phytone medium. Chloroperoxidase was partly purified from the ten cultures. All preparations were glycoproteins, with different carbohydrate content. The absorption spectra of the ten samples were indistinguishable and this was reflected in similar Rz ( / ) values. SDS-PAGE revealed two major bands of protein in all preparations but in different proportions: staining for carbohydrate confirmed these bands to be glycoproteins. PAGE at pH 3 showed each preparation to be composed of several isoenzymes and these could be grouped according to their migration patterns. Kinetic constants, where determined, and pH optima showed no differences among the ten preparations and all exhibited catalase and peroxidase activities in the same relative proportions to chlorinating activity.


Article metrics loading...

Loading full text...

Full text loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error