Two novel GH11 endo-xylanases from Myceliophthora thermophila C1 act differently toward soluble and insoluble xylans

M.P. van Gool, G.C.J. van Muiswinkel, S.W.A. Hinz, H.A. Schols, A.P. Sinitsyn, H. Gruppen

Research output: Contribution to journalArticleAcademicpeer-review

29 Citations (Scopus)

Abstract

Two novel GH11 endo-xylanases from Myceliophthora thermophila C1 (C1), Xyl7 and Xyl8, were purified and the influence of solubility and molecular structure of various xylans on their efficiency was investigated. Both endo-xylanases were hindered by a high degree of substitution of a xylan. The two GH11 xylanases released different products from the xylans, in which Xyl7 displayed a degradation product composition closer to GH10 xylanases. A correlation of the degradation product composition with a specific residue at position 163 in the amino acid sequence of Xyl8 is suggested: tyrosine in Xyl8; valine in Xyl7. This is confirmed with examples of various endo-xylanases reported in literature. The C1 GH11 xylanases were more efficient on self-associated xylan compared to C1 GH10 endo-xylanases and they released more small xylooligomers from these xylans. This is contrary to the general assumption that GH10 xylanases degrade xylans to a higher degree than GH11 xylanases
Original languageEnglish
Pages (from-to)25-32
JournalEnzyme and Microbial Technology
Volume53
Issue number1
DOIs
Publication statusPublished - 2013

Keywords

  • chrysosporium-lucknowense
  • families
  • arabinoxylan
  • hydrolases

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