Open AccessPurification and characterization of a 32‐kDa laccase‐like stilbene oxidase produced by Botrytis cinerea Pers.:Fr.
Author(s) -
Pezet Roger
Publication year - 1998
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.1574-6968.1998.tb13229.x
Subject(s) - botrytis cinerea , laccase , pterostilbene , phytoalexin , resveratrol , chemistry , isoelectric point , botrytis , enzyme , biochemistry , polyphenol oxidase , isoelectric focusing , oxidase test , biology , peroxidase , botany
A 32‐kDa laccase‐like stilbene oxidase was purified to homogeneity (one single band on SDS‐PAGE) from Botrytis cinerea liquid culture medium enriched with pectin. Two major isoforms with p I 4.35 and 4.3 were revealed by isoelectric focusing (IEF). This enzyme oxidizes the grape stilbenic phytoalexins, resveratrol and pterostilbene. Syringaldazine is poorly oxidized by this stilbene oxidase as compared to the rate of stilbene oxidation. This enzyme catalyses the oxidation of resveratrol to ?‐viniferin.