Distinct roles of carbohydrate esterase family CE16 acetyl esterases and polymer-acting acetyl xylan esterases in xylan deacetylation

Sanna Koutaniemi, Martine P van Gool, Minna Juvonen, Jouni Jokela, Sandra W Hinz, Henk A Schols, Maija Tenkanen

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

Sammanfattning

Mass spectrometric analysis was used to compare the roles of two acetyl esterases (AE, carbohydrate esterase family CE16) and three acetyl xylan esterases (AXE, families CE1 and CE5) in deacetylation of natural substrates, neutral (linear) and 4-O-methyl glucuronic acid (MeGlcA) substituted xylooligosaccharides (XOS). AEs were similarly restricted in their action and apparently removed in most cases only one acetyl group from the non-reducing end of XOS, acting as exo-deacetylases. In contrast, AXEs completely deacetylated longer neutral XOS but had difficulties with the shorter ones. Complete deacetylation of neutral XOS was obtained after the combined action of AEs and AXEs. MeGlcA substituents partially restricted the action of both types of esterases and the remaining acidic XOS were mainly substituted with one MeGlcA and one acetyl group, supposedly on the same xylopyranosyl residue. These resisting structures were degraded to great extent only after inclusion of α-glucuronidase, which acted with the esterases in a synergistic manner. When used together with xylan backbone degrading endoxylanase and β-xylosidase, both AE and AXE enhanced the hydrolysis of complex XOS equally.
Originalspråkengelska
TidskriftJournal of Biotechnology
Volym168
Utgåva4
Sidor (från-till)684– 692
Antal sidor9
ISSN0168-1656
DOI
StatusPublicerad - 2013
MoE-publikationstypA1 Tidskriftsartikel-refererad

Vetenskapsgrenar

  • 414 Jordbruksbioteknologi
  • 1182 Biokemi, cell- och molekylärbiologi

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