Assessment of Kaistella jeonii esterase conformational dynamics in response to poly(ethylene terephthalate) binding

The pervasive presence of plastic in the environment has reached a concerning scale, being identified in many ecosystems. Bioremediation is the cheapest and most eco-friendly alternative to remove this polymer from affected areas. Recent work described that a novel cold-active esterase enzyme extracted from the bacteria Kaistella jeonii could promiscuously degrade PET. Compared to the well-known PETase from Ideonella sakaiensis, this novel esterase presents a low sequence identity yet has a remarkably similar folding. However, enzymatic assays demonstrated a lower catalytic efficiency. In this work, we employed a strict computational approach to investigate the binding mechanism between the esterase and PET. Understanding the underlying mechanism of binding can shed light on the evolutive mechanism of how enzymes have been evolving to degrade these artificial molecules and help develop rational engineering approaches to improve PETase-like enzymes. Our results indicate that this esterase misses a disulfide bridge, keeping the catalytic residues closer and possibly influencing its catalytic efficiency. Moreover, we describe the structural response to the interaction between enzyme and PET, indicating local and global effects. Our results aid in deepening the knowledge behind the mechanism of biological catalysis of PET degradation and as a base for the engineering of novel PETases. •Our study explores Kaistella jeonii's esterase catalysis, informing improved PET degradation strategies.•Computational study of a cold-adapted esterase reveals structural responses in enzyme-substrate interaction.•Critical structural and dynamical features are contrasted with the well-established PETase from Ideonella sakaiensis.•Our findings offer a blueprint for the engineering of enzymes with enhanced plastic-degrading capabilities.