Applied Biochemistry and Biotechnology

, Volume 15, Issue 3, pp 213–225

Purification and properties of two laccase isoenzymes produced byBotrytis cinerea

Authors

  • Nabil Zouari
    • Laboratoire de Technologie EnzymatiqueUniversité de Technologie de Compiègne
  • Jean-Louis Romette
    • Laboratoire de Technologie EnzymatiqueUniversité de Technologie de Compiègne
  • Daniel Thomas
    • Laboratoire de Technologie EnzymatiqueUniversité de Technologie de Compiègne
Article

DOI: 10.1007/BF02798450

Cite this article as:
Zouari, N., Romette, J. & Thomas, D. Appl Biochem Biotechnol (1987) 15: 213. doi:10.1007/BF02798450

Abstract

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.

Index Entries

Botrytis cinerealaccasesphenoloxidasesisoenzymesproduction, purification, and characterization of laccase

Copyright information

© Humana Press Inc. 1987