Daniel Kracher
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View article: Continuous and sensitive monitoring of LPMO reactions using an optical H <sub>2</sub> O <sub>2</sub> sensor
Continuous and sensitive monitoring of LPMO reactions using an optical H <sub>2</sub> O <sub>2</sub> sensor Open
Lytic polysaccharide monooxygenases catalyse the H 2 O 2 -dependent cleavage of polysaccharides. An optical H 2 O 2 sensor allows for real-time monitoring of enzyme activity and avoids the determination of oxidised reaction products.
View article: Mechanistic Elucidation and Stereochemical Consequences of Alternative Binding of Alkenyl Substrates by Engineered Arylmalonate Decarboxylase
Mechanistic Elucidation and Stereochemical Consequences of Alternative Binding of Alkenyl Substrates by Engineered Arylmalonate Decarboxylase Open
The cofactor-free arylmalonate decarboxylase (AMDase) is a valuable biocatalyst for synthesizing α-aryl and α-alkenyl alkanoic acids with excellent stereoselectivity. We engineered a new hydrophobic pocket in (S)-selective AMDase mutants, …
View article: Engineering the substrate scope of the thermostable phenolic acid decarboxylase N31 towards sterically hindered phenolic acids
Engineering the substrate scope of the thermostable phenolic acid decarboxylase N31 towards sterically hindered phenolic acids Open
Phenolic acid decarboxylases (PADs) have significant potential for converting bio-based hydroxycinnamic acids (e.g. ferulic acid, p-coumaric acid, caffeic acid, and sinapic acid) into valuable hydroxystyrene monomers. These monomers are in…
View article: Deciphering the evolutionary origin of the enantioselectivity of short-chain dehydrogenases from plants toward 1-borneol
Deciphering the evolutionary origin of the enantioselectivity of short-chain dehydrogenases from plants toward 1-borneol Open
Enzyme engineering has produced numerous methods to optimize enzymes for biotechnological processes; however, less is known about how natural evolution creates new functionalities. We investigate the evolutionary emergence of enantioselect…
View article: Mechanistic elucidation and stereochemical consequences of alternative binding of alkenyl substrates by engineered arylmalonate decarboxylase
Mechanistic elucidation and stereochemical consequences of alternative binding of alkenyl substrates by engineered arylmalonate decarboxylase Open
The cofactor-free arylmalonate decarboxylase (AMDase) is a valuable biocatalyst for synthesizing α-aryl and α-alkenylcarboxylic acids with excellent stereoselectivity. We engineered a new hydrophobic pocket in (S)-selective AMDase variants…
View article: Engineering Substrate Acceptance of Resveratrol <i>O‐</i>Methyltransferase from <i>Vitis vinifera</i> for the Selective Synthesis of <i>O</i>‐Methyl Protected Biobased Hydroxystyrenes
Engineering Substrate Acceptance of Resveratrol <i>O‐</i>Methyltransferase from <i>Vitis vinifera</i> for the Selective Synthesis of <i>O</i>‐Methyl Protected Biobased Hydroxystyrenes Open
Enzymatic decarboxylation of phenolic acids enables the production of biobased phenolic styrenes under mild reaction conditions. However, the free para‐ phenolic group can lead to undesirable side products during polymerization, giving pro…
View article: Engineering substrate acceptance of Resveratrol O-Methyltransferase from Vitis vinifera for the selective synthesis of O-methyl protected biobased hydroxystyrenes
Engineering substrate acceptance of Resveratrol O-Methyltransferase from Vitis vinifera for the selective synthesis of O-methyl protected biobased hydroxystyrenes Open
Enzymatic decarboxylation of phenolic acids enables the production of biobased phenolic styrenes under mild reaction conditions. However, the free para-phenolic group can lead to undesirable side products during polymerization, giving prot…
View article: Discovery and characterization of NADH oxidases for selective sustainable synthesis of 5-hydroxymethylfuran carboxylic acid
Discovery and characterization of NADH oxidases for selective sustainable synthesis of 5-hydroxymethylfuran carboxylic acid Open
Efficient regeneration of NAD+ remains a significant challenge for oxidative biotransformations. In order to identify enzymes with higher activity and stability, a panel of NADH oxidases (Nox) was investigated in the regeneration of nicoti…
View article: Discovery of a Concerted Mechanism in Arylmalonate Decarboxylase Expands the Catalytic Scope for Cofactor-free C-C Bond Cleavage
Discovery of a Concerted Mechanism in Arylmalonate Decarboxylase Expands the Catalytic Scope for Cofactor-free C-C Bond Cleavage Open
The cofactor-free arylmalonate decarboxylase (AMDase) has been applied for the synthesis of a large number of α-aryl and α-alkenylcarboxylic acids with outstanding stereoselectivity. We observed that (S)-selective AMDase variant ICPLLG pro…
View article: Electron Transfer of Cellobiose Dehydrogenase in Polyethyleneimine Films
Electron Transfer of Cellobiose Dehydrogenase in Polyethyleneimine Films Open
Cellobiose dehydrogenase (CDH) is applied as a bioelectrocatalyst in biosensors because its mobile cytochrome domain is capable of direct electron transfer. This study investigates the electron transfer mechanism of CDH molecules embedded …
View article: Active roles of lytic polysaccharide monooxygenases in human pathogenicity
Active roles of lytic polysaccharide monooxygenases in human pathogenicity Open
Lytic polysaccharide monooxygenases (LPMOs) are redox enzymes widely studied for their involvement in microbial and fungal biomass degradation. The catalytic versatility of these enzymes is demonstrated by the recent discovery of LPMOs in …
View article: Stability Increase of Phenolic Acid Decarboxylase by a Combination of Protein and Solvent Engineering Unlocks Applications at Elevated Temperatures
Stability Increase of Phenolic Acid Decarboxylase by a Combination of Protein and Solvent Engineering Unlocks Applications at Elevated Temperatures Open
Enzymatic decarboxylation of biobased hydroxycinnamic acids gives access to phenolic styrenes for adhesive production. Phenolic acid decarboxylases are proficient enzymes that have been applied in aqueous systems, organic solvents, biphasi…
View article: Mapping the Initial Stages of a Protective Pathway that Enhances Catalytic Turnover by a Lytic Polysaccharide Monooxygenase
Mapping the Initial Stages of a Protective Pathway that Enhances Catalytic Turnover by a Lytic Polysaccharide Monooxygenase Open
Oxygenase and peroxygenase enzymes generate intermediates at their active sites which bring about the controlled functionalization of inert C-H bonds in substrates, such as in the enzymatic conversion of methane to methanol. To be viable c…
View article: Spectrophotometric and Fluorimetric High-Throughput Assays for Phenolic Acid Decarboxylase
Spectrophotometric and Fluorimetric High-Throughput Assays for Phenolic Acid Decarboxylase Open
Biocatalytic decarboxylation of hydroxycinnamic acids yields phenolic styrenes, which are important precursors for antioxidants, epoxy coatings, adhesives and other polymeric materials. Bacillus subtilis decarboxylase (BsPAD) is a cofactor…
View article: Spectrophotometric and Fluorimetric High‐Throughput Assays for Phenolic Acid Decarboxylase
Spectrophotometric and Fluorimetric High‐Throughput Assays for Phenolic Acid Decarboxylase Open
Biocatalytic decarboxylation of hydroxycinnamic acids yields phenolic styrenes, which are important precursors for antioxidants, epoxy coatings, adhesives and other polymeric materials. Bacillus subtilis decarboxylase (BsPAD) is a cofactor…
View article: Spectrophotometric and Fluorimetric High-Throughput Assays for Phenolic Acid Decarboxylase
Spectrophotometric and Fluorimetric High-Throughput Assays for Phenolic Acid Decarboxylase Open
Biocatalytic decarboxylation of hydroxycinnamic acids yields phenolic styrenes, which are important precursors for antioxidants, epoxy coatings, adhesives and other polymeric materials. Bacillus subtilis decarboxylase (BsPAD) is a cofactor…
View article: A Cold-Active Flavin-Dependent Monooxygenase from <i>Janthinobacterium svalbardensis</i> Unlocks Applications of Baeyer–Villiger Monooxygenases at Low Temperature
A Cold-Active Flavin-Dependent Monooxygenase from <i>Janthinobacterium svalbardensis</i> Unlocks Applications of Baeyer–Villiger Monooxygenases at Low Temperature Open
Cold-active enzymes maintain a large part of their optimal activity at low temperatures. Therefore, they can be used to avoid side reactions and preserve heat-sensitive compounds. Baeyer-Villiger monooxygenases (BVMO) utilize molecular oxy…
View article: Application of Causality Modelling for Prediction of Molecular Properties for Textile Dyes Degradation by LPMO
Application of Causality Modelling for Prediction of Molecular Properties for Textile Dyes Degradation by LPMO Open
The textile industry is one of the largest water-polluting industries in the world. Due to an increased application of chromophores and a more frequent presence in wastewaters, the need for an ecologically favorable dye degradation process…
View article: Inhibition of the Peroxygenase Lytic Polysaccharide Monooxygenase by Carboxylic Acids and Amino Acids
Inhibition of the Peroxygenase Lytic Polysaccharide Monooxygenase by Carboxylic Acids and Amino Acids Open
Lytic polysaccharide monooxygenases (LPMOs) are widely distributed in fungi, and catalyze the oxidative degradation of polysaccharides such as cellulose. Despite their name, LPMOs possess a dominant peroxygenase activity that is reflected …
View article: The histidine-brace active site of a copper monooxygenase is redox active and forms part of an in-built enzyme repair mechanism
The histidine-brace active site of a copper monooxygenase is redox active and forms part of an in-built enzyme repair mechanism Open
Oxygenase enzymes generate reactive intermediates at their active sites to effect controlled functionalizations of inert C–H bonds in substrates, such as in the enzymatic conversion of methane to methanol. To be viable catalysts, however, …
View article: Recent developments in compartmentalization of chemoenzymatic cascade reactions
Recent developments in compartmentalization of chemoenzymatic cascade reactions Open
Uniting the unparalleled stereoselectivity of enzymes with the efficiency of chemical catalysis offers high product yields and atom economy while limiting downstream processing efforts. However, despite an impressive series of proof-of-con…
View article: Spectroelectrochemical investigation of the glyoxal oxidase activation mechanism
Spectroelectrochemical investigation of the glyoxal oxidase activation mechanism Open
Glyoxal oxidase (GLOX) is an extracellular source of H2O2 in white-rot secretomes, where it acts in concert with peroxidases to degrade lignin. It has been reported that GLOX requires activation prior to catalytic turnover and that a perox…
View article: Insights into the H<sub>2</sub>O<sub>2</sub>‐driven catalytic mechanism of fungal lytic polysaccharide monooxygenases
Insights into the H<sub>2</sub>O<sub>2</sub>‐driven catalytic mechanism of fungal lytic polysaccharide monooxygenases Open
Fungal lytic polysaccharide monooxygenases (LPMOs) depolymerise crystalline cellulose and hemicellulose, supporting the utilisation of lignocellulosic biomass as a feedstock for biorefinery and biomanufacturing processes. Recent investigat…
View article: Chimeric Cellobiose Dehydrogenases Reveal the Function of Cytochrome Domain Mobility for the Electron Transfer to Lytic Polysaccharide Monooxygenase
Chimeric Cellobiose Dehydrogenases Reveal the Function of Cytochrome Domain Mobility for the Electron Transfer to Lytic Polysaccharide Monooxygenase Open
The natural function of cellobiose dehydrogenase (CDH) to donate electrons from its catalytic flavodehydrogenase (DH) domain via its cytochrome (CYT) domain to lytic polysaccharide monooxygenase (LPMO) is an example of a highly efficient e…
View article: Protein Conformational Change Is Essential for Reductive Activation of Lytic Polysaccharide Monooxygenase by Cellobiose Dehydrogenase
Protein Conformational Change Is Essential for Reductive Activation of Lytic Polysaccharide Monooxygenase by Cellobiose Dehydrogenase Open
Large-scale protein domain dynamics and electron transfer are often associated. However, as protein motions span a broad range of time and length scales, it is often challenging to identify and thus link functionally relevant dynamic chang…
View article: Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis
Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis Open
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 s…