Open AccessPresence of a vanadium‐dependent haloperoxidase in Botrytis cinerea
Author(s) -
BarNun Nurit,
Shcolnick Sigal,
Mayer Alfred M
Publication year - 2002
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2002.tb11465.x
Subject(s) - vanadium , botrytis cinerea , enzyme , mycelium , biochemistry , chemistry , extracellular , enzyme assay , molecular mass , glycoprotein , vanadate , gel electrophoresis , microbiology and biotechnology , biology , botany , inorganic chemistry
The presence of a haloperoxidase in the mycelium of Botrytis cinerea , extractable with buffer, is demonstrated. A low level of extracellular enzyme activity was also detected. The haloperoxidase from the fungus is a vanadium‐dependent glycoprotein, with a pH optimum of about 5.5. Native gel electrophoresis indicates that it is a high molecular mass protein. It appears to react with antibodies against haloperoxidase from Caldariomyces fumago . Enzyme activity is increased 3.5‐fold and 15‐fold by culture of the fungus in the presence of NaCl or vanadium, respectively. Activity is partly reduced by removal of vanadium and activity can be restored by the addition of vanadium to the enzyme. The possible function of this haloperoxidase is discussed.