6533b872fe1ef96bd12d39ef
RESEARCH PRODUCT
Characterization of Purified Green Bell Pepper Hydroperoxide Lyase Expressed by Yarrowia Lipolytica: Radicals Detection during Catalysis
Clotilde PolicarJean-marc BelinCatherine VergelyFlorence HussonJean-marc NicaudMirna P. Santiago-gómezLuc Rochettesubject
0106 biological scienceschemistry.chemical_classification0303 health sciencesbiologyRadicalSubstrate (chemistry)BioengineeringYarrowia[CHIM.INOR]Chemical Sciences/Inorganic chemistrybiology.organism_classificationLyase01 natural sciencesApplied Microbiology and BiotechnologyBiochemistryCatalysis03 medical and health sciencesEnzymechemistry010608 biotechnologyPepperOrganic chemistryAlkyl030304 developmental biologyBiotechnologydescription
International audience; The optimization of the expression of recombinant 6-His-tagged HPO lyase in Yarrowia lipolytica is described: 1800U/L of culture was detected at 24h of culture on a medium containing olive oil as the sole carbon source. The enzyme was purified by IMAC and showed an optimal pH at 5.5, an optimal temperature at 20^\circC and a Km value of 9μM with 13-HPOD substrate. The participation of radicals during the catalysis of purified bell pepper fruit hydroperoxide lyase has been observed by electron paramagnetic resonance spectroscopy and the yet unidentified radical species might be an alkyl or alkoxyl radical linked to the enzyme.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2007-07-01 |