A novel, inducible, citral lyase purified from spores of Penicillium digitatum

W.A.M. Wolken, W.J.V. van Loo, J. Tramper, M.J. van der Werf

Research output: Contribution to journalArticleAcademicpeer-review

6 Citations (Scopus)

Abstract

A novel lyase, combining hydratase and aldolase activity, that converts citral into methylheptenone and acetaldehyde, was purified from spores of Penicillium digitatum. Remarkably, citral lyase activity was induced 118-fold by incubating nongerminating spores with the substrate, citral. This cofactor independent hydratase/aldolase, was purified and found to be a monomeric enzyme of 31 kDa. Citral lyase has a Km of 0.058 mm and a Vmax of 52.6 U?mg1. Enzyme activity was optimal at 20 °C and pH 7.6. The enzyme has a strong preference for the trans isomer of citral (geranial). Citral lyase also converts other ,-unsaturated aldehydes (farnesal, methyl-crotonaldehyde, decenal and cinnemaldehyde).
Original languageEnglish
Pages (from-to)5903-5910
JournalEuropean Journal of Biochemistry
Volume269
DOIs
Publication statusPublished - 2002

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