Characterization of an acetyl esterase from Myceliophthorathermophila C1 able to deacetylate xanthan

M.M. Kool, H.A. Schols, M. Wagenknecht, S.W.A. Hinz, B.M. Moerschbacher, H. Gruppen

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Screening of eight carbohydrate acetyl esterases for their activity towards xanthan resulted in the recogni-tion of one active esterase. AXE3, a CAZy family CE1 acetyl xylan esterase originating from Myceliophthorathermophila C1, removed 31% of all acetyl groups present in xanthan after a 48 h incubation. AXE3 activ-ity towards xanthan was only observed when xanthan molecules were in the disordered conformation.Optimal performance towards xanthan was observed at 53¿C in the complete absence of salt, a condi-tion favouring the disordered conformation. AXE3-deacetylated xanthan was hydrolyzed using cellulasesand analyzed for its repeating units using UPLC–HILIC–ELSD/ESI–MS. This showed that AXE3 specificallyremoves the acetyl groups positioned on the inner mannose and that acetyl groups positioned on theouter mannose are not removed at all. After a prolonged incubation at optimal conditions, 57% of allacetyl groups, representing 70% of all acetyl groups on the inner mannose units, were hydrolyzed.
Original languageEnglish
Pages (from-to)222-229
JournalCarbohydrate Polymers
Publication statusPublished - 2014


  • bacterial polysaccharide xanthan
  • xylan esterases
  • carbohydrate esterases
  • xanthomonas-campestris
  • rheological properties
  • plant polysaccharides
  • enzymatic-hydrolysis
  • gum
  • transition
  • families


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