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Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
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Related Experiment Video

Updated: May 27, 2026

Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical (Methylation) and Physical (Mass Spectrometry, Nuclear Magnetic Resonance) Techniques
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GH11 xylanases: Structure/function/properties relationships and applications.

Gabriel Paës1, Jean-Guy Berrin, Johnny Beaugrand

  • 1INRA, UMR614 FARE, 2 esplanade Roland-Garros, F-51686 Reims, France. gabriel.paes@reims.inra.fr

Biotechnology Advances
|November 10, 2011
PubMed
Summary

GH11 xylanases, key enzymes for lignocellulosic biomass breakdown, exhibit high substrate specificity. This review details their structure, catalytic mechanisms, and stability, highlighting their biotechnological potential.

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Published on: September 20, 2016

Area of Science:

  • Biochemistry and Biotechnology
  • Enzyme Engineering
  • Structural Biology

Background:

  • Industrial demand for tailored enzymes has surged due to technical, environmental, and economic drivers.
  • Xylanases, crucial for degrading lignocellulosic plant cell walls, are classified into multiple glycoside hydrolase (GH) families.
  • The GH11 family is particularly noted for its bacterial and fungal members possessing high substrate specificity.

Purpose of the Study:

  • To provide a comprehensive review of GH11 xylanases.
  • To analyze the structure-function relationships of GH11 xylanases.
  • To assess their biochemical properties and biotechnological applications.

Main Methods:

  • Exhaustive analysis of available GH11 xylanase sequences and 3D structures.
  • Correlation of structural data with biochemical properties.
  • Review of existing literature on GH11 xylanase characteristics and applications.

Main Results:

  • Detailed assessment of GH11 xylanase structure, including the critical 'thumb' loop.
  • Analysis of their catalytic machinery, substrate selectivity, and inhibition mechanisms.
  • Evaluation of their stability concerning pH and temperature variations.

Conclusions:

  • GH11 xylanases are well-characterized and highly specific biocatalysts.
  • Their structural features, particularly the 'thumb' loop, are vital for catalytic efficiency.
  • GH11 xylanases are established biotechnological tools with significant potential for future applications.