Directed evolution is widely used to improve enzymes, particularly for industrial biocatalytic
processes. Molecular biology advances present many new strategies for directed evolution. …

Antibody therapies have become an important class of therapeutics in recent years as they
have exhibited outstanding efficacy and safety in the treatment of several major diseases …

Flexible sites are potential targets for engineering the stability of enzymes. Nevertheless,
the success rate of the rigidifying flexible sites (RFS) strategy is still low due to a limited …

The past decade has seen a revolution in our ability to engineer designer enzymes using
genetic tools that mimic evolution on a laboratory timescale. Many excellent examples of …

Microscale processing techniques are rapidly emerging as a means to increase the speed of
bioprocess design and reduce material requirements. Automation of these techniques can …

The engineering of enzymes with altered activity, specificity and stability, using directed
evolution techniques that mimic evolution on a laboratory timescale, is now well established. …

Directed evolution has emerged as a powerful strategy to engineer various properties of
proteins. Traditional methods to construct libraries such as error-prone PCR and DNA shuffling …

Multiple mutations are typically required to significantly improve protein stability or aggregation
kinetics. However, when several substitutions are made in a single protein, the mutations …

The directed evolution of enzymes for improved activity or substrate specificity commonly
leads to a trade-off in stability. We have identified an activity–stability trade-off and a loss in …

The benefits of applying biocatalysts to organic synthesis, such as their high chemo-, regio-,
and enantio-specificity and selectivity, must be seriously considered, especially where …