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

article



Wolken, W.A.M.

Loo, W.J.V. van

Tramper, J.

Werf, M.J. van der
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).
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Carbon-Carbon LyasesChromatography, GelElectrophoresis, Polyacrylamide GelEnzyme InductionEnzyme StabilityHydrogen-Ion ConcentrationMonoterpenesPenicilliumSpores, FungalSubstrate SpecificityTemperatureFungiPenicilliumPenicillium digitatum
TNO Identifier
72875
Repository link
https://resolver.tno.nl/uuid:eda9acb7-fa2e-4893-8517-63190ca9eaa6
ISSN
00142956
Source
European Journal of Biochemistry, 269(23), pp. 5903-5910.
Pages
5903-5910
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