Open AccessPurification and characterization of a 40.8‐kDa cutinase in ungerminated conidia of Botrytis cinerea Pers.: Fr.
Author(s) -
Gindro Katia,
Pezet Roger
Publication year - 1999
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.1574-6968.1999.tb13438.x
Subject(s) - cutinase , botrytis cinerea , cutin , conidium , botrytis , biology , enzyme , biochemistry , botany
Cytoplasmic soluble proteins from ungerminated conidia of Botrytis cinerea exhibited cutinase activity. A 40.8‐kDa cutinase was purified to homogeneity from this crude conidial protein extract. This cutinase does not correspond either to constitutive or to induced lytic cutin enzymes already described by other authors. The possible role of this constitutive cutinase in the induction of other cutinolytic proteins in the early stages of infection of plants by B. cinerea is discussed.