Staff Publications

Staff Publications

  • external user (warningwarning)
  • Log in as
  • language uk
  • About

    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

Record number 413618
Title The ferulic acid esterases of Chrysosporium lucknowense C1: Purification, characterization and their potential application in biorefinery
Author(s) Kuhnel, S.; Pouvreau, L.A.M.; Appeldoorn, M.M.; Hinz, S.W.A.; Schols, H.A.; Gruppen, H.
Source Enzyme and Microbial Technology 50 (2012)1. - ISSN 0141-0229 - p. 77 - 85.
Department(s) Food Chemistry Group
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) sugar-beet pulp - plant-cell walls - aspergillus-niger - maize bran - feruloylated oligosaccharides - structural-characterization - wheat bran - degradation - classification - arabinoxylans
Abstract Three ferulic acid esterases from the filamentous fungus Chrysosporium lucknowense C1 were purified and characterized. The enzymes were most active at neutral pH and temperatures up to 45 °C. All enzymes released ferulic acid and p-coumaric acid from a soluble corn fibre fraction. Ferulic acid esterases FaeA1 and FaeA2 could also release complex dehydrodiferulic acids and dehydrotriferulic acids from corn fibre oligomers, but released only 20% of all ferulic acid present in sugar beet pectin oligomers. Ferulic acid esterase FaeB2 released almost no complex ferulic acid oligomers from corn fibre oligomers, but 60% of all ferulic acid from sugar beet pectin oligomers. The ferulic acid esterases were classified based on both, sequence similarity and their activities toward synthetic substrates. The type A ferulic acid esterases FaeA1 and FaeA2 are the first members of the phylogenetic subfamily 5 to be biochemically characterized. Type B ferulic acid esterase FaeB2 is a member of subfamily 6.
There are no comments yet. You can post the first one!
Post a comment
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.