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  • Unraveling Synergism between Various GH Family Xylanases . . .
    It is noteworthy to mention that GH10 xylanases appeared to have a significant influence on the release of monosaccharides xylose and arabinose by the xylosidase, SXA and arabinofuranosidases during arabinoxylan degradation
  • Characterization of a GH10 extremely thermophilic xylanase . . .
    In this study, only one new xylanase gene sequence (named xyngmqa) with complete domain was obtained from the GMQ metagomic database, which belongs to the GH10 family
  • Glycoside Hydrolase Family 10 - CAZypedia
    Although a few glycoside hydrolases of this family show endo -beta-1,3-xylanase activity, the majority of the enzymes are endo -beta-1,4-xylanases Some of the latter display limited activity on aryl cellobiosides, but not on cellulose
  • Penicillium sp. 由来の新規GH10キシラナーゼはAspergillus β . . .
    A novel GH10 xylanase from Penicillium sp accelerates saccharification of alkaline-pretreated bagasse by an enzyme from recombinant Trichoderma reesei expressing Aspergillus β-glucosidase
  • A novel GH10 xylanase from - Springer
    In this study, we conducted screening of biomass-degrading enzymes that showed synergistic effects with enzyme preparations produced by recombinant T reesei expressing Aspergillus BGL A novel glycoside hydrolase family 10 (GH10) xylanase was obtained from Penicillium sp KSM-F532
  • XynDZ5: A New Thermostable GH10 Xylanase - Frontiers
    In this work, we report the discovery and biochemical characterization of a new thermostable GH10 xylanase, termed XynDZ5, exhibiting only 26% amino acid sequence identity to the closest characterized xylanolytic enzyme
  • Characterization of a novel GH10 xylanase with a . . .
    In this study, the β-1,4-xylanase gene (xyn10A) and its carbohydrate binding module (CBM)-Truncated variant (xyn10A-dC) were cloned from Aspergillus sulphureus JCM01963 and successfully expressed in P pastoris
  • Site-directed mutagenesis of family GH10 Aspergillus . . .
    The study provided preliminary insight into how V99 AfXylA10 and D145 AfXylA10 residue influence enzymatic properties and the interaction with OsXIP These findings might inform design of mutant xylanase with enhanced catalytic activity and reduced sensitivity to xylanase inhibitory proteins (XIs)





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