Feruloyl esterase from aspergillus sp.: purification, properties, and action on natural substrates
An enzyme active toward the methyl ester of ferulic acid was isolated from the fungus Aspergillus sp. and purified to homogeneity using ion-exchange and hydrophobic chromatography. The molecular weight of the enzyme is 42 kD, and its pI is 3.7. The enzyme has a pH optimum in the range 4-6 and a temperature optimum in the range 40 to 60 degrees C. Using a number of synthetic and natural substrates, the enzyme was identified as a feruloyl esterase. The feruloyl esterase did not hydrolyze wheat straw. Ferulic acid was detected as a product of hydrolysis of wheat bran and sugar-beet pulp. Other products were also detected after sugar-beet pulp hydrolysis.
Dzedzyulya
EI
Department of Mycology and Algology, School of Biology, Lomonosov Moscow State University, Moscow, 119899, Russia. kdz@enzyme.chem.msu. su.
Becker
EG
Okunev
ON
Sinitsyn
AP