alexa Purification and characterization of a 40.8-kDa cutinase in ungerminated conidia of Botrytis cinerea Pers.: Fr.
Molecular Biology

Molecular Biology

Journal of Cytology & Histology

Author(s): Gindro K, Pezet R

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Abstract 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.
This article was published in FEMS Microbiol Lett and referenced in Journal of Cytology & Histology

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