top of page



  • Jeppe Kari, Kay Schaller, Gustavo A Molina, Kim Borch and Peter Westh. The Sabatier principle as a tool for discovery and engineering of industrial enzymes (2022), Current Opinion in Biotechnology 78, 102843

  • Schaller, K.S., Molina, G.A., Kari, J., Schiano-Di-Cola, C., Sørensen, T.H., Borch, K., Peters, G.H.J., Westh, P. Virtual Bioprospecting of Interfacial Enzymes: Relating Sequence and Kinetics (2022), ACS Catalysis 12 (12), pp. 7427-7435. 


  • Baath, J.A., Jensen, K., Borch, K., Westh, P., Kari, J. Sabatier Principle for Rationalizing Enzymatic Hydrolysis of a Synthetic Polyester (2022), JACS Au 2 (5) .


  • Kari, J., Molina, G.A., Schaller, K.S., Schiano-di-Cola, C., Christensen, S.J., Badino, S.F., Sørensen, T.H., Røjel, N.S., Keller, M.B., Sørensen, N.R., Kolaczkowski, B., Olsen, J.P., Krogh, K.B.R.M., Jensen, K., Cavaleiro, A.M., Peters, G.H.J., Spodsberg, N., Borch, K., Westh, P. Physical constraints and functional plasticity of cellulases (2021), Nature Communication 12 (1), art. no. 3847


  • Schaller, K.S., Kari, J., Molina, G.A., Tidemand, K.D., Borch, K., Peters, G.H.J., Westh, P. Computing Cellulase Kinetics with a Two-Domain Linear Interaction Energy Approach (2021), ACS Omega 6 (2), pp. 1547-1555. 


  • Keller, M.B., Badino, S.F., Røjel, N., Sørensen, T.H., Kari, J., McBrayer, B., Borch, K., Blossom, B.M., Westh, P. A comparative biochemical investigation of the impeding effect of C1-oxidizing LPMOs on cellobiohydrolases (2021), J. Biol. Chem.  296, art. no. 100504


  • Kari, J., Schiano-Di-Cola, C., Hansen, S.F., Badino, S.F., Sørensen, T.H., Cavaleiro, A.M., Borch, K., Westh, P. A steady-state approach for inhibition of heterogeneous enzyme reactions (2020), Biochemical Journal 447 (10), pp. 1971-1982.

  • Røjel, N., Kari, J., Sørensen, T.H., Borch, K., Westh, P. pH profiles of cellulases depend on the substrate and architecture of the binding region (2020), Biotechnol. Bioeng. 117 (2), pp. 382-391. 


  • Olsen, J.P., Kari, J., Windahl, M.S., Borch, K., Westh, P. Molecular recognition in the product site of cellobiohydrolase Cel7A regulates processive step length (2020), Biochemical Journal  477 (1), pp. 99-110. 


  • Røjel, N., Kari, J., Sørensen, T.H., Badino, S.F., Morth, J.P., Schaller, K., Cavaleiro, A.M., Borch, K., Westh, P. Substrate binding in the processive cellulase Cel7A: Transition state of complexation and roles of conserved tryptophan residues (2020), J. Biol. Chem.  295 (6), pp. 1454-1463. 



  • Kari, J., Christensen, S.J., Andersen, M., Baiget, S.S., Borch, K., Westh, P. A practical approach to steady-state kinetic analysis of cellulases acting on their natural insoluble substrate (2019), Analytical Biochemistry 586, art. no. 113411.


  • Schiano-di-Cola, C., Røjel, N., Jensen, K., Kari, J., Sørensen, T.H., Borch, K., Westh, P. Systematic deletions in the cellobiohydrolase (CBH) Cel7A from the fungus Trichoderma reesei reveal flexible loops critical for CBH activity (2019), J. Biol. Chem.  294 (6), pp. 1807-1815. 



  • Kari, J., Olsen, J.P., Jensen, K., Badino, S.F., Krogh, K.B.R.M., Borch, K., Westh, P. Sabatier Principle for Interfacial (Heterogeneous) Enzyme Catalysis (2018), ACS Catalysis 8 (12), pp. 11966-11972. 


  • Christensen, S.J., Kari, J., Badino, S.F., Borch, K., Westh, P. Rate-limiting step and substrate accessibility of cellobiohydrolase Cel6A from Trichoderma reesei (2018), FEBS J. 285 (23), pp. 4482-4493.


  • Westh, P., Borch, K., Sørensen, T., Tokin, R., Kari, J., Badino, S., Cavaleiro, M.A., Røjel, N., Christensen, S., Vesterager, C.S., Schiano-di-Cola, C. Thermoactivation of a cellobiohydrolase (2018) 115 (4), pp. 831-838. 

  • Borisova, A.S., Eneyskaya, E.V., Jana, S., Badino, S.F., Kari, J., Amore, A., Karlsson, M., Hansson, H., Sandgren, M., Himmel, M.E., Westh, P., Payne, C.M., Kulminskaya, A.A., Ståhlberg, J. Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from trichoderma atroviride, T. Reesei and T. Harzianum (2018) 11 (1)


  • Badino, S.F., Kari, J., Christensen, S.J., Borch, K., Westh, P. Direct kinetic comparison of the two cellobiohydrolases Cel6A and Cel7A from Hypocrea jecorina (2017) 1865 (12), pp. 1739-1745.

  • Olsen, J.P., Kari, J., Borch, K., Westh, P. A quenched-flow system for measuring heterogeneous enzyme kinetics with sub-second time resolution (2017) 105, pp. 45-50.

  • Badino, S.F., Christensen, S.J., Kari, J., Windahl, M.S., Hvidt, S., Borch, K., Westh, P. Exo-exo synergy between Cel6A and Cel7A from Hypocrea jecorina: Role of carbohydrate binding module and the endo-lytic character of the enzymes (2017) 114 (8), pp. 1639-1647. 


  • Kari, J., Andersen, M., Borch, K., Westh, P. An Inverse Michaelis-Menten Approach for Interfacial Enzyme Kinetics (2017). ACS Catalysis 7 (7), pp. 4904-4914. 


  • Kari, J., Kont, R., Borch, K., Buskov, S., Olsen, J.P., Cruyz-Bagger, N., Väljamäe, P., Westh, P. Anomeric selectivity and product profile of a processive cellulase (2017) 56 (1), pp. 167-178. 


  • Sørensen, T.H., Windahl, M.S., McBrayer, B., Kari, J., Olsen, J.P., Borch, K., Westh, P. Loop variants of the thermophile Rasamsonia emersonii Cel7A with improved activity against cellulose (2017) 114 (1), pp. 53-62. 



  • Kont, R., Kari, J., Borch, K., Westh, P., Väljamäe, P. Inter-domain synergism is required for efficient feeding of cellulose chain into active site of cellobiohydrolase cel7A (2016), J. Biol. Chem. 291 (50), pp. 26013-26023.


  • Olsen, J.P., Alasepp, K., Kari, J., Cruys-Bagger, N., Borch, K., Westh, P. Mechanism of product inhibition for cellobiohydrolase Cel7A during hydrolysis of insoluble cellulose (2016), Biotechnol. Bioeng., 113 (6), pp. 1178-1186. 


  • Colussi, F., Sorensen, T.H., Alasepp, K., Kari, J., Cruys-Bagger, N., Windahl, M.S., Olsen, J.P., Borch, K., Westh, P. Probing substrate interactions in the active tunnel of a catalytically deficient cellobiohydrolase (Cel7) (2015), J. Biol. Chem.  290 (4), pp. 2444-2454. 



  • Kari, J., Olsen, J., Borch, K., Cruys-Bagger, N., Jensen, K., Westh, P. Kinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity (2014), J. Biol. Chem. 289 (47), pp. 32459-32468. 

bottom of page