Author

P. Westh

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 5

Signature Assays, Organisms & Methods

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Approach:statistical model· 3 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Research Focus:benchmarking· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Approach:wet-lab / biochemical assay· 1

Frequent Co-Authors

K. Borch· 5 shared K. Jensen· 5 shared J. Brask· 3 shared J. Arnling Baath· 2 shared J. Kari· 2 shared K. Schaller· 2 shared S. Schubert· 2 shared A. M. Cavaleiro· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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5 shared papersBiochemistry

K. Borch

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5 papers

Recent·Most cited

Relationships of crystallinity and reaction rates for enzymatic degradation of poly (ethylene terephthalate), PET

S. Schubert, T. T. Bach, K. S. Clausen, A. Malmendal, C. J. Hunt, K. Borch, K. Jensen, J. Brask, A. S. Meyer, P. Westh

The paper investigates how crystallinity affects enzymatic degradation of PET, finding that high crystallinity limits enzyme activity due to conformational constraints and reduces productive sites on the polymer surface.

bioRxiv · Nov 5, 2023Biochemistry

Reaction pathways for the enzymatic degradation of poly(ethylene terephthalate): What characterizes an efficient PET-hydrolase?

S. Schubert, K. Schaller, J. A. Baath, C. Hunt, K. Borch, K. Jensen, J. Brask, P. Westh

The paper identifies endo-lytic activity as a key determinant of PET hydrolase efficiency by analyzing reaction pathways and enzyme kinetics.

bioRxiv · Sep 13, 2022Biochemistry

Sabatier principle for rationalizing enzymatic hydrolysis of a synthetic polyester

J. Arnling Baath, K. Jensen, K. Borch, P. Westh, J. Kari

The paper applies the Sabatier principle to analyze PET hydrolase kinetics, showing that optimal turnover occurs at intermediate enzyme-PET binding strength, with implications for enzyme design and process optimization.

bioRxiv · Mar 30, 2022 · PreprintBiochemistry

Comparative biochemistry of four polyester (PET) hydrolases

J. Arnling Baath, K. Borch, K. Jensen, J. Brask, P. Westh

The paper compares four PET hydrolases using a kinetic framework to assess their efficiency and substrate affinity.

bioRxiv · Nov 20, 2020Biochemistry

Physical constrains and functional plasticity of cellulases: Linear scaling relationships for a heterogeneous enzyme reaction

J. Kari, G. Molina, K. Schaller, S. Christensen, C. Schiano-di-Cola, S. Badino, T. Soerensen, N. Roejel, M. Keller, B. Kolaczkowski, J. P. Olsen, K. Krogh, K. Jensen, A. M. Cavaleiro, G. H. Peters, , P. Westh

The paper characterizes 83 cellulases, revealing a linear free energy relationship between substrate binding strength and activation barrier, suggesting physical constraints and evolutionary optimization in interfacial enzyme catalysis.

bioRxiv · May 20, 2020 · PreprintBiochemistry