Directed evolution, enzyme design, and effective immobilization have been used to improve the catalytic activity. Dynamic polymers offer a promising platform to improve enzyme activity in aqueous solutions. Here, amphiphilic dynamers and lipase self-assemble into nanoparticles of 150- to 600-nanometer diameter, showing remarkable threefold enhancement in catalytic activity. In addition, they also demonstrated the ability to promote the reversible refolding of the partially or completely denatured lipase. The catalytic efficiency is completed with its more convenient handling of dynameric nanoparticles facilitating the efficient recovery and reuse of the enzyme with cost-effective uses. Molecular simulation studies revealed an in-depth understanding of how the dynamer action mechanism affects the conformational changes of lipase. The dynamer served as an effective hydrophobic support, facilitating the lid opening and substrate access to the catalytic triad, resulting in a substantial activation with an improved stability and recyclability of the lipase.
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