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. 2002;94(1):29-33.
doi: 10.1263/jbb.94.29.

Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1

Lies Dwiarti  1 , Ken Yamane, Hitoshi Yamatani, Prihardi Kahar, Mitsuyasu Okabe
Affiliations

Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1

Lies Dwiarti et al. J Biosci Bioeng. 2002.

Abstract

cis-Aconitic acid decarboxylase (CAD) was assumed to be a key enzyme in the production of itaconic acid by comparing the activity of CAD from Aspergillus terreus TN484-M1 with that of CAD from the low-itaconate yielding strain Aspergillus terreus CM85J. The constitutive CAD was purified to homogeneity from A. terreus TN484-M1 by ammonium sulfate fractionation, and column chromatography on DEAE-toyopearl, Butyl-toyopearl, and Sephacryl S200HR, and then characterized. A molecular mass of 55 kDa for the native enzyme was determined by SDS-PAGE. The enzymic activity was optimal at a pH of 6.2 and temperature of 45 degrees C. The K(m) value for cis-aconitic acid was determined as 2.45 mM (pH 6.2, 37 degrees C). The enzyme was completely inactivated by Hg+, Cu2+, Zn2+, p-chloromercuribenzoate, and 5,5'-dithio-bis(2-nitrobenzoate).

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