6533b7d1fe1ef96bd125d78f

RESEARCH PRODUCT

Isolation and characterization of a chlorogenic acid esterase from Aspergillus niger.

B. SchöbelW. Pollmann

subject

chemistry.chemical_classificationChromatographybiologyIsoelectric focusingSwineAspergillus nigerbiology.organism_classificationEsteraseGeneral Biochemistry Genetics and Molecular BiologyEnzyme assayIsoenzymesMolecular Weightchemistry.chemical_compoundHydrolysisKineticsEnzymeChlorogenic acidchemistryLiverCaffeic acidbiology.proteinAnimalsAspergillus nigerCarboxylic Ester Hydrolases

description

Abstract The isolation and characterization of a specific chlorogenic acid esterase is described. The enzyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means of ultrafiltration and column-chromatography. The pH- and temperature optimum were 6.5 and 45 °C respectively. Divalent cations were not required for the enzyme activity. As other esterases, this enzyme is inhibited by di-isopropyl-phosphorofluoridate. The Km-value is 0.70 mᴍ chlorogenic acid, the molecular weight 240000. The described enzyme is specific for chlorogenic acid. On the other hand a typical unspecific esterase like the pig liver esterases does not split chloro­genic acid. The isoelectric focusing reveals several isoenzymes of chlorogenase within a pI-range of 4.0-4.5.

yearjournalcountryeditionlanguage
1980-03-01Zeitschrift fur Naturforschung. Section C, Biosciences
10.1515/znc-1980-3-407https://pubmed.ncbi.nlm.nih.gov/7385941