About
Sebastian Jannick Muderspach is a Guest Researcher in the Department of Chemistry at the University of Copenhagen's Faculty of Science. His work centers on structural and functional analysis of carbohydrate-active enzymes, with expertise in lytic polysaccharide monooxygenases (LPMOs) and galactanases. Affiliated with the Lo Leggio research group, he utilizes X-ray crystallography and protein engineering to investigate enzyme mechanisms.
His research interests focus on enzyme structure-function relationships, particularly in polysaccharide degradation systems. Key areas include the histidine brace motif in copper-dependent oxygenases, substrate binding dynamics in GH53 galactanases, and engineering thermostable variants for industrial applications. His work bridges fundamental enzymology with biocatalyst development for biomass conversion.
Analysis of his 9 publications (2019-2023) reveals a consistent focus on structural enzymology of carbohydrate-active proteins, with dominant subfields including LPMO mechanisms (AA9/AA13 families), GH53 galactanase engineering, and copper coordination chemistry. His most cited works address oxidative cellulose degradation and high-resolution structural insights into catalytic histidine residues.
- PhD in Chemistry (2023) from University of Copenhagen
- ORCID: 0000-0002-7032-6941
Muderspach collaborates extensively with structural biology groups across Europe, particularly with Prof. Lo Leggio's team. His research leverages X-ray crystallography, mutagenesis, and biochemical assays to characterize enzyme mechanisms. Current work emphasizes protein engineering for improved biocatalysts in biomass processing, with applications in sustainable biofuel production.
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