A novel, inducible, citral lyase purified from spores of Penicillium digitatum
van Loo, W.J.V.
van der Werf, M.J.
Centraal Instituut voor Voedingsonderzoek TNO
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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Electrophoresis, Polyacrylamide Gel
European Journal of Biochemistry, 269 (23), 5903-5910