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Applying Conformational Dynamics in Enzyme Evolution to Biocatalysis

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Biocatalysis is a green and sustainable tool for production of fine chemicals. One of the main benefits is that enzymes can catalyze reactions with high selectivity, allowing to reduce the need to complex separation processes. Additionally, it will provide a more sustainable and environmentally friendly alternative to traditional chemical catalysis. Enzymes can operate under mild reaction conditions, which can reduce energy consumption and waste production.

In some cases, to match industrial conditions and performances, biocatalysts may require increased
enzyme stability, catalytic efficiency, selectivity, or substrate scope. Therefore, enzyme engineering may be a necessary solution to enhance the characteristics of natural enzymes to reach such high efficiency
requirements. Enzyme evolution involves some changes of amino acid residues that constitute the sequence of the protein, which can alter its conformational dynamics and ultimately affect its enzymatic function. Even, the change of only one amino acid may drastically improve or alter the enzyme activity!
In this article, we provide the benefits of using rational-design and semi-rational approach for enzyme
evolution. We also highlight some of our work carried out in collaboration with Compbiolab Group.


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