Results 61 to 70 of about 2,233 (191)
Advanced Science, Volume 13, Issue 47, 24 August 2026.The diagram illustrates a sustainable model of lignin valorization and carbon cycling based on microbial cell factories. Using lignin as the feedstock, synthetic biology technologies, including depolymerization, cell factory construction, pathway gene module integration, and metabolic network regulation, are applied to convert lignin into bulk ...
Na Li +4 more
wiley +1 more source
Mimicking the Reactivity of LPMOs with a Mononuclear Cu Complex
European Journal of Inorganic ChemistryAbstractLytic polysaccharide monooxygenases (LPMOs) are Cu‐dependent metalloenzymes that catalyze the hydroxylation of strong C−H bonds in polysaccharides using O2 or H2O2 as oxidants (monooxygenase/peroxygenase). In the absence of C−H substrate, LPMOs reduce O2 to H2O2 (oxidase) and H2O2 to H2O (peroxidase) using proton/electron donors.
Kundan Sagar +7 more
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Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis
Biomolecules, 2020 Lytic polysaccharide monooxygenases (LPMOs) are industrially important oxidoreductases employed in lignocellulose saccharification. Using advanced time-resolved mass spectrometric techniques, we elucidated the structural determinants for substrate ...
Frantisek Filandr +6 more
doaj +1 more source
Functional characterization of a lytic polysaccharide monooxygenase from the thermophilic fungus Myceliophthora thermophila. [PDF]
PLoS ONE, 2018 Thermophilic fungi are a promising source of thermostable enzymes able to hydrolytically or oxidatively degrade plant cell wall components. Among these enzymes are lytic polysaccharide monooxygenases (LPMOs), enzymes capable of enhancing biomass ...
Marco A S Kadowaki +8 more
doaj +1 more source
Investigations on dielectric resonators for applications below 1 GHz
Archives of Acoustics, 2014 This paper is concerned with the design and analysis of UHF dielectric resonators operating below 1GHz in certain applications where quartz-based acoustic resonators of modest performance or metallic cavities are customary employed. Lowest-order modes of
M. VALENTIN, R. E. ELCHEIKH
doaj
AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes
Biotechnology for Biofuels, 2019 Background Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance.
Camille Filiatrault-Chastel +10 more
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BMC Microbiology, 2022 Background Aliivibrio salmonicida is the causative agent of cold-water vibriosis in salmonids (Oncorhynchus mykiss and Salmo salar L.) and gadidae (Gadus morhua L.). Virulence-associated factors that are essential for the full spectrum of A.
Anna Skåne +8 more
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Acta Biochimica et Biophysica Sinica, 2023 Along with long-term evolution, the plant cell wall generates lignocellulose and other anti-degradation barriers to confront hydrolysis by fungi. Lytic polysaccharide monooxygenase (LPMO) is a newly defined oxidase in lignocellulosic degradation systems ...
Yu Xinran +3 more
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Insights Into Divergent Mechanisms of Pyrite Oxidation by Indigenous Fungi From Mine Tailings
Microbial Biotechnology, Volume 19, Issue 8, August 2026.To elucidate the mechanisms of fungal pyrite oxidation, a large‐scale isolation of indigenous pyrite‐oxidizing fungi from mine tailings was conducted, and three focal strains were subjected to integrated multi‐omics and molecular analysis in fungus‐pyrite co‐culture systems, revealing their divergent oxidative strategies.
Yu‐xiang Li +10 more
wiley +1 more source
The discovery of novel LPMO families with a new Hidden Markov model [PDF]
BMC Research Notes, 2017 Renewable biopolymers, such as cellulose, starch and chitin are highly resistance to enzymatic degradation. Therefore, there is a need to upgrade current degradation processes by including novel enzymes. Lytic polysaccharide mono-oxygenases (LPMOs) can disrupt recalcitrant biopolymers, thereby enhancing hydrolysis by conventional enzymes.
Voshol, G., Vijgenboom, E., Punt, P.
openaire +3 more sources