Enzymatic Characterization of Lytic Polysaccharide Monooxygenase TtLPMO9Y and Its Role in Juice Clarification and Cellulose Degradation [PDF]
Shipin KexueA novel lytic polysaccharide monooxygenase, TtLPMO9Y, was cloned and expressed from Thermothelomyces thermophilus. Its enzymatic properties were characterized, and its role in the degradation process of cellulose and pectin in plant cell walls was ...
LI Cong, NIU Yufeng, ZHAO Guozhu, ZHENG Fei
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Estimating the accuracy of calculated electron paramagnetic resonance hyperfine couplings for a lytic polysaccharide monooxygenase [PDF]
Computational and Structural Biotechnology Journal, 2021 Lytic polysaccharide monooxygenases (LPMOs) are enzymes that bind polysaccharides followed by an (oxidative) disruption of the polysaccharide surface, thereby boosting depolymerization.
Yusuf A. Theibich +3 more
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The impact of the carbohydrate-binding module on how a lytic polysaccharide monooxygenase modifies cellulose fibers [PDF]
Biotechnology for Biofuels and BioproductsBackground In recent years, lytic polysaccharide monooxygenases (LPMOs) that oxidatively cleave cellulose have gained increasing attention in cellulose fiber modification.
Fredrik G. Støpamo +8 more
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A Designed Copper Histidine-Brace Enzyme for Oxidative Depolymerization of Polysaccharides as a Model of Lytic Polysaccharide Monooxygenase [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2023 Casey Van Stappen +2 more
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Dose-dependent structural and electron-density features in the lytic polysaccharide monooxygenase NcAA9D. [PDF]
Acta Crystallogr D Struct BiolA series of 36 structures of the Neurospora crassa LPMO NcAA9D were refined against X‐ray crystal datasets collected with increasing dose from a single crystal to provide insights into dose‐dependent structural changes at the active site of the enzyme.
Miller SA, O'Dell WB, Meilleur F.
europepmc +2 more sources
Experimental estimation of copper-site geometry reproducibility in biologically relevant redox and saccharide-bound states of a model lytic polysaccharide monooxygenase. [PDF]
Acta Crystallogr D Struct BiolSmall but measurable changes in the coordination geometry of a lytic polysaccharide monooxygenase copper active site are revealed by X‐ray crystallography, providing structural insight into their catalytic flexibility.Lytic polysaccharide monooxygenases (LPMOs) are copper‐dependent enzymes classified into the auxiliary activity (AA) families of the ...
Huang Z +7 more
europepmc +2 more sources
Enzymatic activity of lytic polysaccharide monooxygenase
, 2016 The present invention is in the area of enzymes for (hemi-)cellulose degradation and/or modification, more in particular the degradation and/or modification of xylan.
Visser, Jaap +5 more
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Improving the Enzymatic Activity and Stability of a Lytic Polysaccharide Monooxygenase. [PDF]
Int J Mol Sci, 2023 Lytic Polysaccharide Monooxygenases (LPMOs) are copper-dependent enzymes that play a pivotal role in the enzymatic conversion of the most recalcitrant polysaccharides, such as cellulose and chitin. Hence, protein engineering is highly required to enhance their catalytic efficiencies.
Berhe MH, Song X, Yao L.
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On the expansion of biological functions of lytic polysaccharide monooxygenases [PDF]
New Phytologist, 2022 SummaryLytic polysaccharide monooxygenases (LPMOs) constitute an enigmatic class of enzymes, the discovery of which has opened up a new arena of riveting research. LPMOs can oxidatively cleave the glycosidic bonds found in carbohydrate polymers enabling the depolymerisation of recalcitrant biomasses, such as cellulose or chitin. While most studies have
Theruvothu Madathil Vandhana +5 more
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Understanding the initial events of the oxidative damage and protection mechanisms of the AA9 lytic polysaccharide monooxygenase family [PDF]
, 2023 Lytic polysaccharide monooxygenase (LPMO) is a new class of oxidoreductases that boosts polysaccharide degradation employing a copper active site.
Marlisa M., Hagemann +2 more
core +1 more source