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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 Q 10  is 1.5, the activation energy E A  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.

zeitschrift für naturforschung c

Weitere Charakterisierung einer Chlorogensäure-Hydrolase aus Aspergillus niger / Further Characterization of a Chlorogenic Acid Hydrolase from Aspergillus niger