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

ABSTRACT: 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

SUBMITTER: Pinto ESM 

PROVIDER: S-EPMC10885555 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature