6533b7d6fe1ef96bd12671b1
RESEARCH PRODUCT
Purification of hydroperoxide lyase from green bell pepper (Capsicum annuum L.) fruits for the generation of C6-aldehydes in vitro.
F HussonJean-marc Belinsubject
Lipid PeroxidesProtein DenaturationChloroplastsLinolenic AcidsBioconversionBiologyAldehydechemistry.chemical_compoundBiosynthesisCytochrome P-450 Enzyme SystemPolyacrylamide gel electrophoresisAldehyde-Lyaseschemistry.chemical_classificationAldehydesChromatographyPlant ExtractsGeneral ChemistryLyasebiology.organism_classificationChromatography Ion ExchangeChloroplastMolecular WeightEnzymechemistryBiochemistryLinoleic AcidsChromatography GelElectrophoresis Polyacrylamide GelGeneral Agricultural and Biological SciencesCapsicumSolanaceaedescription
The aim of this work was to compare the efficiency of different extracts of hydroperoxide lyase from green bell peppers in producing aldehydes: a crude extract, a chloroplastic fraction, and a purified enzyme were investigated. From a crude extract, the HPO lyase was purified by ion-exchange chromatography with a 22.3-fold increase in purification factor. Analysis by SDS-PAGE electrophoresis under denaturating conditions showed only one protein with a molecular weight of 55 kDa, whereas size-exclusion chromatography indicated a molecular weight of 170 kDa. A maximum of 7500 mg of aldehydes per g of protein was obtained with the purified enzyme within 20 min of bioconversion compared to 392 and 88 mg of aldehydes per g of protein within 50 and 60 min, respectively, for the chloroplast fraction and the crude extract.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2002-02-26 | Journal of agricultural and food chemistry |