Purification and properties of two laccase isoenzymes produced byBotrytis cinerea

Laccases produced by five strains ofBotrytis cinerea were studied. Extraction and purification have been performed in order to compare the enzymatic characteristics both, physicochemically and kinetically. Two strains produced isoenzymes of laccase. These two molecular forms of laccase had different isoelectric points (2.6 and 2.8) and sugar content (86 and 91%). The optimum reactional pH was found to be very similar for both enzymes, in contrast to the temperature sensitivity, which is very different.