Comparative characterization of deletion derivatives of the modular xylanase XynA of Thermotoga maritima

No abstract is available for this paper.

• Publication year

  2006

• Venue

  Extremophiles

• Publication date

  2006-03-21

• Fields of study

  Biology, Medicine, Materials Science, Chemistry

• Identifiers
  DOI 10.1007/s00792-006-0509-0PMID 16550304
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Fusion of family 2b carbohydrate‐binding module increases the catalytic activity of a xylanase from Thermotoga maritima to soluble xylan

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• Characterization of XYN10B, a modular xylanase from the ruminal protozoan Polyplastron multivesiculatum, with a family 22 carbohydrate-binding module that binds to cellulose.

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  2001cited by this paper
• Identification of novel beta-mannan- and beta-glucan-binding modules: evidence for a superfamily of carbohydrate-binding modules.

  2001cited by this paper
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  2001cited by this paper
• Importance of the Carbohydrate-Binding Module of Clostridium stercorarium Xyn10B to Xylan Hydrolysis

  2001cited by this paper
• Molecular characterization of xynX, a gene encoding a multidomain xylanase with a thermostabilizing domain from Clostridium thermocellum

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  1999cited by this paper
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  1998cited by this paper
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  1997cited by this paper
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  1996cited by this paper
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  1996cited by this paper
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  1996cited by this paper
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  1995cited by this paper
• Two Extremely Thermostable Xylanases of the Hyperthermophilic Bacterium Thermotoga maritima MSB8

  1995influential reference
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• A New Group of Modular Xylanases in Glycoside Hydrolase Family 8 from Marine Bacteria

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• Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass

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