<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9</volume><submitter>Cai L</submitter><pubmed_abstract>Enzyme-assisted valorization of lichenan represents a green and sustainable alternative to the conventional chemical industry. The recently discovered lytic polysaccharide monooxygenases (LPMOs) are essential components of state-of-the-art enzyme cocktails for lichenin bioconversion. The LPMOs named SpyTag fused LPMOs (AST) from &lt;i>Chaetomium globosum&lt;/i> was functionally expressed in &lt;i>E. coli&lt;/i> and exhibited 1.25-fold synergism with lichenase, whereas AST alone produced no detectable reducing sugars. HPLC results further confirm that AST does not alter the endogenous hydrolysis mode of lichenase but rather enhances its hydrolysis efficiency by disrupting the long chain of lichenan and releasing more reducing ends. To the best of our knowledge, this was the first report on the synergis</pubmed_abstract><journal>Frontiers in nutrition</journal><pagination>970540</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9626761</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>The synergism of lytic polysaccharide monooxygenases with lichenase and their co-immobilization on silica nanospheres for green conversion of lichen biomass.</pubmed_title><pmcid>PMC9626761</pmcid><pubmed_authors>Zhang G</pubmed_authors><pubmed_authors>Zheng Y</pubmed_authors><pubmed_authors>Liu L</pubmed_authors><pubmed_authors>Chu Y</pubmed_authors><pubmed_authors>Cai L</pubmed_authors><pubmed_authors>Lin Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>The synergism of lytic polysaccharide monooxygenases with lichenase and their co-immobilization on silica nanospheres for green conversion of lichen biomass.</name><description>Enzyme-assisted valorization of lichenan represents a green and sustainable alternative to the conventional chemical industry. The recently discovered lytic polysaccharide monooxygenases (LPMOs) are essential components of state-of-the-art enzyme cocktails for lichenin bioconversion. The LPMOs named SpyTag fused LPMOs (AST) from &lt;i>Chaetomium globosum&lt;/i> was functionally expressed in &lt;i>E. coli&lt;/i> and exhibited 1.25-fold synergism with lichenase, whereas AST alone produced no detectable reducing sugars. HPLC results further confirm that AST does not alter the endogenous hydrolysis mode of lichenase but rather enhances its hydrolysis efficiency by disrupting the long chain of lichenan and releasing more reducing ends. To the best of our knowledge, this was the first report on the synergis</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2025-04-27T01:39:52.273Z</modification><creation>2024-11-05T22:05:48.127Z</creation></dates><accession>S-EPMC9626761</accession><cross_references><pubmed>36337671</pubmed><doi>10.3389/fnut.2022.970540</doi></cross_references></HashMap>