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Interfacial molecular interactions of cellobiohydrolase Cel7A and its variants on cellulose.

Akshata R MudinoorPeter M GoodwinRaghavendra U RaoNardrapee KarunaAlex HitomiJennifer NillTina Jeoh
Published in: Biotechnology for biofuels (2020)
Cel7A binding to cellulose is driven by the interactions between the catalytic domain and cellulose. The cellulose-binding module (CBM) and linker increase the affinity of Cel7A to cellulose likely by facilitating recognition and complexation at the substrate interface. The increased affinity of Cel7A to cellulose by the CBM and linker comes at the cost of increasing the population of immobilized enzyme on cellulose. The residence time (or inversely the dissociation rates) of Cel7A on cellulose is not catalysis limited.
Keyphrases
  • ionic liquid
  • aqueous solution
  • silver nanoparticles
  • mass spectrometry
  • molecular dynamics simulations
  • dna binding
  • amino acid