Weitere Charakterisierung einer Chlorogensäure-Hydrolase aus Aspergillus niger / Further Characterization of a Chlorogenic Acid Hydrolase from Aspergillus niger
| Autor: | B. Schöbel, W. Pollmann |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
chemistry.chemical_classification
biology Stereochemistry Chemistry Sodium Aspergillus niger chemistry.chemical_element biology.organism_classification General Biochemistry Genetics and Molecular Biology Enzyme assay chemistry.chemical_compound Enzyme Biochemistry Chlorogenic acid Mole Hydrolase biology.protein Polyacrylamide gel electrophoresis |
| Zdroj: | Zeitschrift für Naturforschung C. 35:699-701 |
| ISSN: | 1865-7125 0939-5075 |
| Popis: | In addition to our previous paper [1] further characteristics of the chlorogenic acid hydrolase are described. Polyacrylamid gelelectrophoresis revealed only one band for the purified enzyme. Sodium dodecyl-sulfate polyacrylamid gelelectrophoresis showed a molecular weight of 60000, demonstrating four subunits of the enzyme (total molecular weight 240000). The enzyme is stable in a pH-range of 3 .0 -8 .5 and up to a temperature of 55 °C. The temperature coefficient Q10 is 1.5, the activation energy EA is 6.0 kcal/mol. The amino acid analysis and substrate specificity data are given in tables. Essential for the enzyme activity is the C=C double bound neighbouring the ester linkage. The enzyme crystallizes in prisms. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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