An actinobacteria lytic polysaccharide monooxygenase acts on both cellulose and xylan to boost biomass saccharification.

ABSTRACT:

Background

Lytic polysaccharide monooxygenases (LPMOs) opened a new horizon for biomass deconstruction. They use a redox mechanism not yet fully understood and the range of substrates initially envisaged to be the crystalline polysaccharides is steadily expanding to non-crystalline ones.

Results

The enzyme KpLPMO10A from the actinomycete Kitasatospora papulosa was cloned and overexpressed in Escherichia coli cells in the functional form with native N-terminal. The enzyme can release oxidized species from chitin (C1-type oxidation) and cellulose (C1/C4-type oxidation) similarly to other AA10 members from clade II (subclade A). Interestingly, KpLPMO10A also cleaves isolated xylan (not complexed with cellulose, C4-type oxidation), a rare activity amo

SUBMITTER: Correa TLR 

PROVIDER: S-EPMC6509861 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature