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

Citation
K. Gindro et R. Pezet, Purification and characterization of a 40.8-kDa cutinase in ungerminated conidia of Botrytis cinerea Pers.: Fr., FEMS MICROB, 171(2), 1999, pp. 239-243
Citations number
23
Categorie Soggetti
Microbiology
Journal title
FEMS MICROBIOLOGY LETTERS
ISSN journal
03781097 → ACNP
Volume
171
Issue
2
Year of publication
1999
Pages
239 - 243
Database
ISI
SICI code
0378-1097(19990215)171:2<239:PACOA4>2.0.ZU;2-#
Abstract
Cytoplasmic soluble proteins from ungerminated conidia of Botrytis cinerea exhibited cutinase activity. A 40.8-kDa cutinase was purified to homogeneit y from this crude conidial protein extract. This cutinase does not correspo nd either to constitutive or to induced lytic cutin enzymes already describ ed by other authors. The possible role of this constitutive cutinase in the induction of other cutinolytic proteins in the early stages of infection o f plants by B. cinerea is discussed. (C) 1999 Federation of European Microb iological Societies. Published by Elsevier Science B.V. All rights reserved .