| | 1 | Author
| Abteilung Biochemie, C.H Boehringer Sohn | Requires cookie* | | | Title
| B. Schöbel und W. Pollmann  | | | | Abstract
| 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 o f the enzyme (total molecular weight 240000). The enzyme is stable in a pH-range of 3 .0 -8 .5 and up to a temperature o f 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. Weitere Charakterisierung einer Chlorogensäure-Hydrolase aus Aspergillus niger | | | |
Reference
| Z. Naturforsch. 35c, 699—701 (1980); eingegangen am 12. Mai/20. Juni 1980 | | | |
Published
| 1980 | | | |
Keywords
| Chlorogenic Acid Hydrolase, Aspergillus niger, Polyacrylamid Gelelectrophoresis, Amino Acid Analysis, Substrate Specificity | | | |
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| default:Reihe_C/35/ZNC-1980-35c-0699.pdf | | | | Identifier
| ZNC-1980-35c-0699 | | | | Volume
| 35 | |
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