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Cellulosomal expansin: functionality and incorporation into the complex.

Lior Artzi1, Ely Morag1, Melina Shamshoum1

  • 1Department of Molecular Biosciences, The Weizmann Institute of Science, Rehovot, Israel.

Biotechnology for Biofuels
|March 15, 2016
PubMed
Summary
This summary is machine-generated.

Clostridium clariflavum expansin-like protein CclEXL1 enhances cellulose degradation by binding to microcrystalline cellulose and improving enzymatic hydrolysis. This finding implicates CclEXL1 in biomass deconstruction and suggests pretreatment benefits.

Keywords:
CellulasesCellulose degradationCellulosomesClostridium clariflavumCohesinDockerinPlant cell wall looseningTensile strength

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Area of Science:

  • Microbiology
  • Biochemistry
  • Biotechnology

Background:

  • Expansins are plant and microbial proteins that disrupt cell walls by interfering with polysaccharide bonding.
  • Clostridium clariflavum, a plant cell wall-degrading bacterium, possesses an elaborate cellulosomal system.
  • Two expansin-like proteins, CclEXL1 and CclEXL2, were identified in C. clariflavum, with CclEXL1 integrated into the cellulosome system.

Purpose of the Study:

  • To analyze the functionality of the C. clariflavum expansin-like protein CclEXL1.
  • To investigate the role of CclEXL1 within the bacterial cellulosome system.
  • To determine the impact of CclEXL1 on cellulose hydrolysis and biomass deconstruction.

Main Methods:

  • Characterization of CclEXL1's dockerin binding to cohesins.
  • Experimental analysis of CclEXL1's binding affinity to various cellulosic and non-cellulosic substrates.
  • Assessment of CclEXL1's effect on the mechanical properties of filter paper.
  • Evaluation of CclEXL1's impact on enzymatic hydrolysis by C. clariflavum cellulosomes and specific cellulases.

Main Results:

  • CclEXL1's dockerin selectively binds to type-I cohesins, including those from C. clariflavum (ScaG) and C. cellulolyticum.
  • CclEXL1 exhibits preferential binding to microcrystalline cellulose and also interacts with acid-swollen cellulose, xylan, and wheat straw.
  • CclEXL1 significantly loosens filter paper, reducing its tensile stress.
  • CclEXL1 markedly enhances the enzymatic hydrolysis of cellulose by C. clariflavum cellulosomes and major cellulases (GH48 and GH9).

Conclusions:

  • The C. clariflavum expansin-like protein CclEXL1 is an integral component of the cellulosome system, contributing to cellulose degradation.
  • CclEXL1 demonstrates cellulose creeping capabilities.
  • Pretreatment of cellulosic materials with CclEXL1 can substantially improve subsequent hydrolysis by cellulases, indicating potential applications in biomass deconstruction.