Cellulases adsorb reversibly on biomass lignin.

ABSTRACT: Adsorption of cellulases onto lignin is considered a major factor in retarding enzymatic cellulose degradation of lignocellulosic biomass. However, the adsorption mechanisms and kinetics are not well understood for individual types of cellulases. This study examines the binding affinity, kinetics of adsorption, and competition of four monocomponent cellulases of Trichoderma reesei during adsorption onto lignin. TrCel7A, TrCel6A, TrCel7B, and TrCel5A were radiolabeled for adsorption experiments on lignin-rich residues (LRRs) isolated from hydrothermally pretreated spruce (L-HPS) and wheat straw (L-HPWS), respectively. On the basis of adsorption isotherms fitted to the Langmuir model, the ranking of binding affinities was TrCel5A >  TrCel6A >  TrCel7B >  TrCel7A on both types of LRRs. The en

SUBMITTER: Djajadi DT 

PROVIDER: S-EPMC6282830 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature