English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

Cost-efficient plant biomass conversion using biochemical and/or chemical routes is essential for transitioning to sustainable chemical technologies and renewable biofuels. Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that make part of modern hydrolytic cocktails destined for plant biomass degradation. Here, we characterized MtLPMO9A from Thermothelomyces thermophilus M77 (formerly Myceliophthora thermophila) and demonstrated that it could be efficiently driven by chlorophyllin excited by light in the presence of a reductant agent. However, in the absence of chemical reductant, chlorophyllin and light alone do not lead to a significant release of the reaction products by the LPMO, indicating a low capacity of MtLPMO9A reduction (either via direct electron transfer or via superoxide ion, O2•-). We showed that photocatalysis could significantly increase the LPMO activity against highly crystalline and recalcitrant cellulosic substrates, which are poorly degraded in the absence of chlorophyllin and light. We also evaluated the use of co-substrates by MtLPMO9A, revealing that the enzyme can use both hydrogen peroxide (H2O2) and molecular oxygen (O2) as co-substrates for cellulose catalytic oxidation.

biofuel research journal

Combining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase MtLPMO9A