| 1 | Author
| B. Schöbel, W. Pollmann | Requires cookie* | | Title
| Isolation and Characterization of a Chlorogenic Acid Esterase from Aspergillus niger  | | | Abstract
| The isolation and characterization o f a specific chlorogenic acid esterase is described. The en zyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means o f ultrafiltration and column-chromatography. The pH-and tempe rature optimum were 6.5 and 45 °C respectively. Divalent cations were not required for the en zyme activity. As other esterases, this enzyme is inhibited by di-isopropyl-phosphorofluoridate. TTie Ä Tm-value is 0.70 mM 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 chloro genic acid. The isoelectric focusing reveals several isoenzymes o f chlorogenase within a pl-range o f 4 .0 -4 .5 . | | |
Reference
| Z. Naturforsch. 35c, 209 (1980); received November 20 1979/January 17 1980 | | |
Published
| 1980 | | |
Keywords
| Chlorogenic Acid Esterase, Aspergillus niger, High Performance Thin Layer Chromatography | | |
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| default:Reihe_C/35/ZNC-1980-35c-0209.pdf | | | Identifier
| ZNC-1980-35c-0209 | | | Volume
| 35 | |
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