Search bioRxiv⌕ Search

Biology subjects

Nintzel, F.

Publications and source records attributed to Nintzel, F..

2 recordsLinked to original sources

Microdroplet screening rapidly profiles a biocatalyst to enable its AI-assisted engineering

Engineering enzymes for increased efficiency is key to enabling sustainable, green biocatalytic production processes in the chemical and pharmaceutical industries. This challenge can be tackled from two angles: by directed evolution, based on labour-intensive experimental testing of enzyme variant libraries, or by computational methods, where data-dependent algorithms relating sequence and function are used to predict biocatalyst improvements. Here, we combine both approaches into a two-week, low-cost workflow, in which ultra-high throughput screening of a library of imine reductases (IREDs) in microfluidic devices provides not only selected hits, but also long-read sequence data linked to fitness scores of >17 thousand enzyme variants. We demonstrate the engineering of an IRED for chiral amine synthesis by mapping its local fitness landscape in one go, ready to be used for interpretation and extrapolation by protein engineers with the help of machine learning (ML). We calculate position-dependent mutability and combinability scores of mutations and comprehensively illuminate a complex interplay of mutations driven by synergistic, often positively epistatic effects. When interpreted by easy-to-use regression and tree-based ML algorithms designed for random whole-gene mutagenesis data, 3-fold improved hits initially obtained from experimental screening are extrapolated further to give another order of magnitude improvement (23-fold in kcat) after testing only a handful of designed mutants. Predictions succeed in >80% of cases. The catalytic features discovered in one IRED are shown to be portable and confer activity on IREDs with [~]50% homology. Our campaigns yield biocatalytically efficient IREDs and are paradigmatic for future enzyme engineering efforts that rely on large sequence-function maps, profiling how a biocatalyst responds to mutation. In the age of predictive biology, these maps will chart the way to improved function by exploiting the synergy of rapid experimental screening combined with ML evaluation and extrapolation.

synthetic biology↗

Ultrahigh throughput evolution of tryptophan synthase in droplets via an aptamer-biosensor

Tryptophan synthase catalyzes the synthesis of a wide array of non-canonical amino acids and is an attractive target for directed evolution. Droplet microfluidics offers an ultrahigh throughput approach to directed evolution (>107 experiments per day), enabling the search for biocatalysts in wider regions of sequence space with reagent consumption minimized to the picoliter volume (per library member). While the majority of screening campaigns in this format on record relied on an optically active reaction product, a new assay is needed for tryptophan synthase. Tryptophan is not fluorogenic in the visible light spectrum and thus falls outside the scope of conventional droplet microfluidic read-outs which are incompatible with UV light detection at high throughput. Here, we engineer a tryptophan DNA aptamer into a biosensor to quantitatively report on tryptophan production in droplets. The utility of the biosensor was validated by identifying 5-fold improved tryptophan synthases from [~]100,000 protein variants. More generally this work establishes the use of DNA-aptamer sensors with a fluorogenic read-out in widening the scope of droplet microfluidic evolution.

biochemistry↗