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Hydrolysis of Nonpolar n-Alkyl Ferulates by Feruloyl Esterases.
Journal article

Hydrolysis of Nonpolar n-Alkyl Ferulates by Feruloyl Esterases.

  • Schär A Institute of Food, Nutrition and Health, ETH Zurich , Schmelzbergstrasse 9, CH-8092 Zurich, Switzerland.
  • Sprecher I Institute of Food, Nutrition and Health, ETH Zurich , Schmelzbergstrasse 9, CH-8092 Zurich, Switzerland.
  • Topakas E Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens , 5 Iroon Polytechniou Str., Zografou Campus, 15700 Athens, Greece.
  • Faulds CB Aix Marseille Université , INRA BBF UMR_A 1163 Biodiversité et Biotechnologie Fongiques, 13288 Marseille cedex 02, France.
  • Nyström L Institute of Food, Nutrition and Health, ETH Zurich , Schmelzbergstrasse 9, CH-8092 Zurich, Switzerland.
  • 2016-09-08
Published in:
  • Journal of agricultural and food chemistry. - 2016
A. niger feruloyl esterase
C. thermocellum feruloyl esterase
R. miehei lipase
alkyl ferulates
ferulic acid
feruloyl esterase
Aspergillus niger
Carboxylic Ester Hydrolases
Coumaric Acids
Fungal Proteins
Hydrolysis
Kinetics
English Ferulic acid is one of the major phenolic acids in plants and can be found esterified to plant cell wall components, but also as long-chain n-alkyl and steryl esters. Microbial feruloyl esterases may play a role in the bioavailability of phenolic acids during human and animal digestion. It is therefore of interest if feruloyl esterases are capable of hydrolyzing nonpolar ferulic acid esters. A series of n-alkyl ferulates with increasing lipophilicity were enzymatically synthesized, and the kinetic constants of their hydrolysis by four feruloyl esterases and a lipase as control were determined. A decrease in Km and kcat could be observed with decreased substrate polarity for all of the feruloyl esterases. Only one feruloyl esterase and the control lipase showed hydrolytic activity toward octadecyl ferulate. These results led to the conclusion that lipophilic ferulates are poor substrates for known feruloyl esterases and more specific esterases/lipases need to be identified.
Language
  • English
Open access status
closed
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Persistent URL
https://sonar.ch/global/documents/104411
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