A novel, inducible, citral lyase purified from spores of Penicillium digitatum.
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 degrees C and pH 7.6. The enzyme has a strong preference for the trans isomer of citral (geranial). Citral lyase also converts other alpha,beta-unsaturated aldehydes (farnesal, methyl-crotonaldehyde, decenal and cinnemaldehyde).
Wolken
Wout A M
WA
Division of Industrial Microbiology, Department of Food Technology and Nutritional Sciences, Wageningen University, the Netherlands. wout.wolken@imb.ftns.wau.nl
Van Loo
Willem J V
WJ
Tramper
Johannes
J
Van Der Werf
Mariët J
MJ
D000080462:Acyclic Monoterpenes; D019755:Carbon-Carbon Lyases / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D039821:Monoterpenes / Q000378:metabolism; D010407:Penicillium / Q000201:enzymology* / Q000502:physiology; D013172:Spores, Fungal / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
D000080462:Acyclic Monoterpenes; D039821:Monoterpenes; D019755:Carbon-Carbon Lyases; C459588:citral lyase; C007076:citral