[Further characterization of a chlorogenic acid hydrolase from Aspergillus niger (author's transl)]

Z Naturforsch C Biosci. Sep-Oct 1980;35(9-10):699-701.
[Article in German]

Abstract

In addition to our previous paper [1] further characteristics of the chlorogenic acid hydrolase are described. Polyacrylamide gel electrophoresis revealed only one band for the purified enzyme. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis showed a molecular weight of 60 000, demonstrating four subunits of the enzyme (total molecular weight 240 000). The enzyme is stable in a pH-range of 3.0--8.5 and up to a temperature of 55 degrees 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.

MeSH terms

  • Aspergillus niger / enzymology*
  • Calorimetry
  • Carboxylic Ester Hydrolases / isolation & purification
  • Carboxylic Ester Hydrolases / metabolism*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Weight
  • Substrate Specificity

Substances

  • Carboxylic Ester Hydrolases
  • chlorogenic acid esterase