Vincent G. H. Eijsink

The paper shows that copper(I)-binding domains in LPMOs from intestinal pathogens are linked to virulence and copper homeostasis in the gut.

The paper develops a fluorescent probe-based method to screen plastic-degrading enzymes using rhodamine-doped polymer substrates and validates it with PET and polyethylene materials.

The paper identifies a catalytic activity in a fungal expansin-like protein, challenging the traditional view of ERPs as non-catalytic.

This study investigates how evolutionary pressures shaped LPMO enzymes to enhance redox robustness through copper re-oxidation and radical scavenging mechanisms.

The paper functionally characterizes multi-domain LPMOs from marine Vibrio species, revealing that domain-domain interactions modulate enzyme activity by regulating copper site accessibility.

This paper improves the genome assembly of Onygena corvina using a hybrid sequencing approach, resulting in a more complete and contiguous genome with enhanced gene annotations.

The paper discovers and characterizes a new family of bacterial heme-thiolate peroxygenases, showing structural and functional similarities to eukaryotic UPOs.

This study identifies the keratinolytic machinery of Onygena corvina, revealing a diverse set of enzymes and mechanisms for keratin degradation, with enhanced efficiency on mixed substrates.

The paper identifies a copper-binding CBM2 module that regulates LPMO activity by scavenging free copper and interacting with the LPMO's catalytic site, preventing oxidative damage.

This study attempts to replicate two recent claims of enzymatic degradation of polyethylene and poly(vinyl chloride) but finds no activity under various conditions, suggesting previous results may have been misinterpreted.