Altering the linker in processive GH5 endoglucanase 1 modulates lignin binding and catalytic properties.

ABSTRACT:

Background

The non-productive adsorption of cellulases onto lignin in biomass is a key issue for the biofuel process economy. It would be helpful to reduce the inhibitory effect of lignin on enzymatic hydrolysis by engineering weak lignin-binding cellulases. Cellulase linkers are highly divergent in their lengths, compositions, and glycosylations. Numerous studies have revealed that linkers can facilitate optimal interactions between structured domains. Recently, efforts have focused on the contributions and mechanisms of carbohydrate-binding modules and catalytic domains that affect lignin affinity and processivity of cellulases, but our understanding of the effects of the linker regions on lignin adsorption and processivity of GH5 processive endoglucanases is still limited.

Re

SUBMITTER: Wang Z 

PROVIDER: S-EPMC6297974 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature