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

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Author: Wolken, W.A.M. · Loo, W.J.V. van · Tramper, J. · Werf, M.J. van der
Type:article
Date:2002
Institution: Centraal Instituut voor Voedingsonderzoek TNO
Source:European Journal of Biochemistry, 23, 269, 5903-5910
Identifier: 72875
doi: doi:10.1046/j.1432-1033.2002.03312.x
Keywords: Nutrition · Carbon-Carbon Lyases · Chromatography, Gel · Electrophoresis, Polyacrylamide Gel · Enzyme Induction · Enzyme Stability · Hydrogen-Ion Concentration · Monoterpenes · Penicillium · Spores, Fungal · Substrate Specificity · Temperature · Fungi · Penicillium · Penicillium digitatum

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·mg-1. 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 α,β-unsaturated aldehydes (farnesal, methyl-crotonaldehyde, decenal and cinnemaldehyde).