Engineering Enzymes for Environmental Sustainability

Abstract

The development and implementation of more efficient and sustainable technologies is key to delivering our net‐zero targets. Here we review how engineered enzymes, with a focus on those developed using directed evolution, can be deployed to improve the sustainability of numerous processes and help to conserve our environment. Efficient and robust biocatalysts have been engineered to capture carbon dioxide (CO2) and have been embedded into new efficient metabolic CO2 fixation pathways. Enzymes have been refined for bioremediation, enhancing their ability to degrade toxic and harmful pollutants. Biocatalytic recycling is gaining momentum, with engineered cutinases and PETases developed for the depolymerization of the abundant plastic, PET. Finally, biocatalytic approaches for accessing petroleum‐based feedstocks and chemicals are expanding, using optimized enzymes to convert plant biomass into biofuels or other high value products. Through these examples, we hope to illustrate how enzyme engineering and biocatalysis can contribute to the development of more environmentally sustainable approaches, in order to protect our planet.

Protein Representations: Encoding Biological Information for Machine Learning in Biocatalysis

“…In the current time of climate change and increasing resource depletion, enzyme technology has emerged as a more environmentally friendly and potentially low-impact approach to industrial processes traditionally mediated by conventional chemistry (Buller et al, 2023;Hauer, 2020;Radley et al, 2023;Reetz et al, 2024;Sheldon and Woodley, 2018;Wu et al, 2021). Instead of complicated pathways with a plethora of reagents, extreme conditions, and protection groups, enzymes offer a renewable alternative with high selectivity and tunability (Sheldon and Woodley, 2018;Woodley, 2022;Wu et al, 2021).…”

Enhancing enzymatic activity with nanoparticle display – an updated compendium and engineering outlook

“…1–5 There are several different approaches to achieving such enhancement, some of which have been applied independently or even jointly, and these include looking for more permissive or active enzyme homologs from other source species, mutational selection and/or evolution for optimized versions of the enzyme itself, and parametric adjustment of overall components and reaction conditions in a multienzyme cascade within a design of experimental framework. 6–16 Interestingly, attaching enzymes to macroscale scaffolds such as surfaces, beads, and resins can help increase an enzyme's structural stability and, in turn, it's viable lifetime providing for long-term application along with potential reuse by allowing for the attached enzymes to be removed with the scaffolding and added to another reaction. 17,18 However, the latter is not normally pursued to enhance enzyme activity such as the catalytic rate or k cat , for example, primarily because chemical attachment to macroscale scaffolding materials is usually achieved with a concomitant decrease in that enzyme's kinetic properties.…”

Sub-single-turnover quantification of enzyme catalysis at ultrahigh throughput via a versatile NAD(P)H coupled assay in microdroplets

“…Enzyme engineering campaigns rely on functional screening for the discovery of initial hits and subsequent directed evolution [1] . In light of the increasing demand for biocatalysts in the transition towards a sustainable bioeconomy [2] , sensitive and high-throughput-compatible assays are crucial for overcoming the challenges arising from target functions that are hard to find in screening libraries to sample the proverbial vastness of sequence space [3,4] in a timeefficient manner [5,6] .…”