Chemical and thermal stability of ferulic acid (feruloyl) esterases from Aspergillus

C. B. Faulds, F. O. Aliwan, R. Vries, R. W. Pickersgill, J. Visser, G. Williamson

Research output: Chapter in Book/Report/Conference proceedingChapter (Book)Researchpeer-review

6 Citations (Scopus)


Ferulic acid (feruloyl) esterases are a novel subclass of the carboxylic acid esterases, and are able to hydrolyze esterified phenolic acids from plant cell walls. The active sites of feruloyl esterases show high homology with the serine active sites of lipases, and a model of a feruloyl esterase (FAE-III) from Aspergillus niger was derived based on the structure of four lipases. Stability of this feruloyl esterase was compared to a feruloyl esterase from A. tubingensis using chemical and thermal denaturation. These enzymes show a 92.5% identity in their amino acid sequences. The A. tubingensis feruloyl esterase is more sensitive to degradation than the A. niger FAE-III. These enzymes have potential in the food and agro-chemical industries.

Original languageEnglish
Title of host publicationStability and Stabilization of Biocatalyst
Subtitle of host publicationProceedings of an International Symposium organized under auspices of the Worldng Party on Applied Biocatalysis of the European Federation of Biotechnology, the University of Cordoba, Spain, and the Spanish Society of Biotechnology Cordoba, Spain, April 19-22, 1998
Place of PublicationNetherlands
Number of pages6
ISBN (Print)0444829709
Publication statusPublished - 1 Dec 1998
Externally publishedYes

Publication series

NameProgress in Biotechnology
ISSN (Print)0921-0423

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