Feruloyl Esterase from Aspergillus sp.: Purification, Properties, and Action on Natural Substrates

E. I. Dzedzyulya¹, E. G. Becker^2*, O. N. Okunev³, and A. P. Sinitsyn²

¹Department of Mycology and Algology, School of Biology, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-0997; E-mail: kdz@enzyme.chem.msu.su

²Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-0997; E-mail: lbecker@enzyme.chem.msu.su

³Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia; fax: (095) 923-3602; E-mail: okunev@ibpm.serpukhov.su

^* To whom correspondence should be addressed.

Received June 11, 1998; Revision received July 3, 1998

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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°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.

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KEY WORDS: ferulic acid methyl ester, feruloyl arabinoside, feruloyl esterase, sugar-beet pulp, wheat bran, wheat straw

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