Towards better biocatalysts: advances in high throughput screening and data-driven design of immobilized enzymes

corresponding

DAVID ROURA PADROSA
CEO and co-founder, inSEIT AG, Bern, Switzerland

 

Abstract

Enzyme immobilization is a critical technology to enhance the stability and reusability of biocatalysts for industrial applications. However, traditional immobilization development is still tied to trial-and-error approaches, which are time-consuming and often lead to a suboptimal preparation. In this article, we aim to discuss the latest developments in the integration of high throughput experimentation, bioinformatics and data driven tools for the design and development of novel immobilized enzymes.


Introduction

 

Biocatalysis has been for the last couple of decades, a focus area for the development of new synthetic strategies. The excellent selectivity that enzymes exhibit makes them valuable catalysts for the synthesis of key chiral intermediates, complex molecules and in late-stage functionalization (1, 2).

 

Biocatalysis, however, apart from for selected productions, has not experienced the broad applicability that could be expected. The two main reasons behind this are the intrinsic (in)stability and (in)compatibility of enzymes under industrial conditions and the long development times and costs associated with the development of tailored solutions (3). For industrial integration, biocatalysis must necessarily co-exist with organic chemistry in a synthetic route, and the two should be easy to implement into the same multi-step synthesis. However, these two technologies tend to operate in very different conditions - for biocatalysis, typically, the main solvent is water, and the reaction conditions are mild (20-40°C, atmospheric pressure). Organic synthesis, on the other hand, is typically performed in organic ...