Publications

Members of the COST Action COZYME publish in renowned academic journals. This page contains articles that result from the joint work of two or more Action members and their collaborators.

BOOK OF ABSTRACTS

Working group meeting
April 16th–17th, 2026
Belgrade, Serbia

Mobilizing the Biocatalysis Community for Reproducible and Reusable Data Collection

Marques S. M. Planas-Iglesias J., Velecký J., Musil M., Asano Y., Borowski T., Brissos V., Cespug M., Chorozian K., Dadashipour M., Erdem E., Ferrandi E. E., Grigorakis K., Kluza A., Lawniczek J., Makryniotis K., Monti D., Nestl B., Ngo A. C., Nikolaivits E., Patti S., Pentari C., Rodrigues C. F., Schopper T., Seweryn-Ożóg K., Szaleniec M., Taborda A., Tataruch M., Tischler D., Topakas E., Wang J., Wójcik P, Wojtkiewicz A. M., Woodley J. M., Zastawny O., Martins L. O., Fraaije M. W., Pleiss J., Schnell S., Damborsky J., Mazurenko S., Bedna D.
ACS Catalysis, 2026.

https://pubs.acs.org/doi/10.1021/acscatal.5c07904

Enzymes for synthesis and degradation of bio-based polyesters: automatic in silico screening and experimental validation

Todea, A., Fortuna, S., Vattovaz, D., di Stefano, D., Carosati, E., Vlad, M., Gardossi, L. ChemSusChem, 2026, 19, e202502311.
https://doi.org/10.1002/cssc.202502311Digital Object Identifier (DOI)

 

Reduced Processivity in a Chitobiohydrolase Enhances LPMO-Assisted Chitin Depolymerization

Votvik A. K., Forsberg Z., Gautieri A., Eijsink V. G. H., Sørlie M.
Biochemistry  2026, 65, 5, 591-602.

https://www.cell.com/iscience/fulltext/S2589-0042(25)02518-0

Accessible biocatalyst development by rapid in vitro semi-rational engineering (RISE) of enzymes

Telek A., Zsolt Gaják V., Dargó G., Mičan J., Bednář D., Vértessy B. G., Tasnádi G. iScience, 2026,  29, 1, 114257.

https://www.cell.com/iscience/fulltext/S2589-0042(25)02518-0

 

Regioselective Sesquiterpene Hydroxylation Directed by Tunnel Remodeling in Rieske Oxygenases

Berger J. B., Marques S. M., Wissner J. L.,  Schelle J. T., Beekwilder J., Damborsky J., Bernhard H. JACS Au, 6, 2026, 847-857.

https://pubs.acs.org/doi/10.1021/jacsau.5c01130

FireProtDB 2.0: large-scale manually curated database of the protein stability data

Musil M., Simeon Borko S., Planas-Iglesias  J., Lacko D, Rosinska M., Kabourek P., Martins O. L., Tataruch M., Damborsky J., Mazurenko S., Bednar D. Nucleic Acids Research, 54, 2026, D409–D418.
https://doi.org/10.1093/nar/gkaf1211

Artificial Metalloenzymes

Editor: Palomo J.M.
https://link.springer.com/book/10.1007/978-3-032-04810-3

Structure–Function Analysis of an Understudied Type of LPMO with Unique Redox Properties and Substrate Specificity

Hall K. R., Rønnekleiv S. E., Gautieri A., Lilleås H., Skaali R., Rieder L.,  Englund A. N., Landsem E., Emrich-Mills T. Z., Ayuso-Fernández I., Røhr Å. K., Sørlie M., Eijsink V. G. H. ACS Catalysis 2025, 15(12), 10601-10617. https://doi.org/10.1021/acscatal.5c03003
 

Development of a highly active engineered PETase enzyme for polyester degradation

Bhattacharya S., Castagna R., Estiri H., Upmanis T., Ricci A., Gautieri A., Parisini E. The FEBS Journal 2025, 293, 443-445.  
https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/febs.70228
 

Integrating Computational and Experimental Methods for the Rational Ecodesign and Synthesis of Functionalized Safe and Sustainable Biobased Oligoesters

Zappaterra F., Todea A., Asaro F., Ditalia P.F.A., Danielli C., Renzi M., Anselmi S., Gardossi L. Polymers 2025, 17, 2537.  
 

Decoding Protein Stabilization: Impact on Aggregation, Solubility, and Unfolding Mechanisms

Havlásek M., Marques S. M., Szotkowská V., Kunka A.,  Babková P., Damborský J., Prokop Z., Bednář D. J. Chem. Info. Model. 2025, 65, 8688-8701.  

https://pubs.acs.org/doi/10.1021/acs.jcim.5c00611

 

Biochemical and Computational Characterization of Haloalkane Dehalogenase Variants Designed by Generative AI: Accelerating the SN2 Step

Gelfand N., Vojtech O., Cui W., Damborský J., Li C., Prokop Z., Xie W. J, Warshel A. J. Am. Chem. Soc. 2025, 147, 2747-2755.  

https://pubs.acs.org/doi/10.1021/jacs.4c15551 

Engineering Dehalogenase Enzymes Using Variational Autoencoder-Generated Latent Spaces and Microfluidics

Pavel Kohout P., Vasina M., Majerova M., Novakova V., Damborsky J., Bednar D., Marek M., Prokop Z., Mazurenko S. JACS Au 2025, 5, 838-850.  
https://pubs.acs.org/doi/10.1021/jacsau.4c01101

Colloidal Protein–Silver Nanoparticle Metalloenzyme as Artificial Redox Biocatalyst

Bojanov G., Garcia-Sanz C., Palomo J.M. Catalysts, 2025, 15, 61. 

https://www.mdpi.com/2073-4344/15/1/61

Developing and improving enzyme-driven technologies to synthesise emerging prebiotics

Green Chem.  2025, 27, 8777-8803.

https://pubs.rsc.org/en/content/articlelanding/2025/gc/d5gc01723h

 

Network Dynamics as Fingerprints of Thermostability in an In Silico-Engineered DyP-Type Peroxidase

Rodrigues C. F.,  Silva D., Lorena C., Borges P. T., Masgrau L., Martins O. L.
ACS Catalysis 2025, 15, 15395-15409. 

https://pubs.acs.org/doi/full/10.1021/acs.jcim.5c01983

Best Practices for Machine Learning-Assisted Protein Engineering

Herrera-Rocha F., Medina-Ortiz D., Mauz F., Pleiss J.,  Davari M.M.  J. Chem. Inf. Model.  2025, 65, 23. 

https://pubs.acs.org/doi/full/10.1021/acs.jcim.5c01983

Recombinant napin expression in Pichia pastoris: Structural and functional attributes in comparison with canola-derived napin

Shemesh P., Cai H., Barzallo-Mora R.-R., Maršavelski A., Fishman A., Int. J. Biol. Macromol. 2025, 322, 146676.

https://www.sciencedirect.com/science/article/pii/S0141813025072332?via%3Dihub

Allosteric regulation of L-lactate dehydrogenase: Beyond effector-mediated tetramerization

Cai H., Shulami S., Štefanić Z., Hrenar T., Maršavelski A., Fishman A., Protein. Sci. 2025, 34, 70206.

https://pubmed.ncbi.nlm.nih.gov/40563163/

BOOK OF ABSTRACTS

Working group meeting
April 24th–25th, 2025
Athens, Greece

Structural and Mechanistic Characterization of the Flavin-Dependent Monooxygenase and Oxidase Involved in Sorbicillinoid Biosynthesis

Dehydrogenase versus oxidase function: the interplay between substrate binding and flavin microenvironment

Biochemical and structural insights into pinoresinol hydroxylase from Pseudomonas sp.

Broadening the Catalytic Scope of the Peroxygenase Activity of a Bacterial Tyrosine Hydroxylase

Design of a gold nanoparticles site
in an engineered lipase: an artificial metalloenzyme with enantioselective
reductase-like activity.

Artificial manganese metalloenzymes with
laccase-like activity: design, synthesis, and characterization.

Zinc Nanobiohybrids for the Photocatalytic Conversion of CO2 to Bicarbonate

Efficient biotransformation of biobased raw materials into novel polyesters/polyesteramides; comparative investigation of enzymatic synthesis of block and random copolymers and terpolymers

Reactive natural deep eutectic solvents increase selectivity and efficiency of lipase catalyzed esterification of carbohydrate polyols

Enzymatic Synthesis and Structural Modeling of Bio-Based Oligoesters as an Approach for the Fast Screening of Marine Biodegradation and Ecotoxicity.

Lipase-catalysed esterification in a reactive natural deep eutectic solvent leads to lauroylcholine chloride rather than glucose ester

New model compounds for the efficient colorimetric screening of medium chain length polyhydroxyalkanoate (mcl-PHA) depolymerases reveal mechanism of activity

Nenadović, M., Maršavelski, A., Škaro Bogojević, S., Maslak, V., Nikodinovć-Runić, J., Milovanović. J., International Journal of Biological Macromolecules, 2024, 283, 137672. 

https://doi.org/10.1016/j.ijbiomac.2024.137672

The STRENDA Biocatalysis Guidelines for cataloguing metadata

CANDy: Automated analysis of domain architectures in carbohydrate-active enzymes

Protein representations: Encoding biological information for machine learning in biocatalysis

Unlocking Catalytic Diversity of a Formate Dehydrogenase: Formamide Activity for NADPH Regeneration and Amine Supply for Asymmetric Reductive Amination

Structure, mechanism, and evolution of the last step in vitamin C biosynthesis

Boverio A., Jamil N., Mannucci B., Mascotti M.L., Fraaije M.W., Mattevi A., Nat. Commun. 2024, 15, 4158.  https://pubs.acs.org/doi/10.1021/acs.biochem.4c00320

Biosynthetic Strategies of Berberine Bridge Enzyme-like Flavoprotein Oxidases toward Structural Diversification in Natural Product Biosynthesis

Evolution, structure, and drug-metabolizing activity of mammalian prenylcysteine oxidases

Distal mutations enhance efficiency of free and immobilized NOV1 dioxygenase for vanillin synthesis

Biomimetic CO2 Capture Unlocked through Enzyme Mining: Discovery of a Highly Thermo- and Alkali-Stable Carbonic Anhydrase

Rigkos K., Filis G., Antonopoulou I., de Oliveira Maciel A., Saridis P., Zarafeta D, Skretas G.
Environmental Science & Technology, 2024 58, 17732-17742.
 

BOOK OF ABSTRACTS

COZYME meeting at University of Zagreb Faculty of Science //

Enzymatic detection of histamine: Applications, challenges, and improvement potential through biocatalyst engineering

Rodríguez-Núñez, K., Serey, M., Pastén, M-J., Bernal, C., Ensari, Y., Davari, M. D., Martinez, R.,  Food Control, 2024, 162, 110436.
https://doi.org/10.1016/j.foodcont.2024.110436.

 

Fluent Integration of Laboratory Data into Biocatalytic Process Simulation Using EnzymeML, DWSIM, and Ontologies

Behr, A. S., Surkamp, J., Abbaspour, E., Häußler, M., Lütz, S., Pleiss, J., Kockmann, N., Rosenthal, K., Processes, 2024, 12, 597.

https://doi.org/10.3390/pr12030597  

Discovery and biochemical characterization of thermostable glycerol oxidases

Santema, L.L., Rotilio, L., Xiang, R., Tjallinks, G., Guallar, V., Mattevi, A., Fraaije, M.W., Appl. Microbiol. Biotechnol., 2024, 108, 61.

https://doi.org/10.1007/s00253-023-12883-9

Exploring new galaxies: Perspectives on the discovery of novel PET-degrading enzymes

Mican, J., Jaradat, D. M. M., Liu, W., Weber, G., Mazurenko, S., Bornscheuer, U. T., Damborsky, J., Wei, R., Bednar. D., Applied Catalysis B: Environmental , 2024, 342, 123404. 

https://doi.org/10.1016/j.apcatb.2023.123404

Tailoring FPOX enzymes for enhanced stability and expanded substrate recognition

Estiri, H., Bhattacharya, S., Buitrago, J.A.R.. Castagna, R., Legzdina, L., Casucci, G., Ricci, A., Parisini, E., Gautieri, A., Scientific Reports, 2023, 13, 18610.

https://doi.org/10.1038/s41598-023-45428-1

Modulating Substrate Specificity of Rhizobium sp. Histamine Dehydrogenase through Protein Engineering for Food Quality Applications

Rodríguez-Núñez, K., Cortés-Monroy, A., Serey, M., Ensari, Y., Davari, M.D., Bernal, C., Martinez, R., Molecules, 2023, 28, 3748.

https://doi.org/10.3390/molecules28093748

Brave new surfactant world revisited by thermoalkalophilic lipases: computational insights into the role of SDS as a substrate analog

Shehata, M., Unlu, A., Iglesias-Fernandez, J., Osuna, S., Sezerman, O. U., Timucin, E., PhysChemChemPhys, 2023, 25, 2234-2247.

EnzymeML: seamless data flow and modeling of enzymatic data

Curse and Blessing of Non-Proteinogenic Parts in Computational Enzyme Engineering

Machine Learning-Guided Protein Engineering