Out of the dark.Into the reactor.
We find industrial enzymes in microbes from extreme environments, then test them in 3D water simulations before synthesis.
- Ready for lab production
- DNA blueprints formatted for standard microbial expression; codon-optimized cassettes
- Tested in simulated water
- 3D active-site, water-stability, and binding-energy simulations before synthesis
- Confidential partner testing
- Test on your own material under bilateral CDA/MTA; option fees credit 100% toward a license
Lead candidates
Eight enzyme, peptide, and protein leads available for confidential partner testing. Select any candidate to inspect its 3D structure, active site, and development stage.
Ambient PFAS defluorinase (DB-PFAS1)
PFAS (“forever chemicals”) resist conventional water treatment short of incineration. Selected from 1.26M environmental sequences, this candidate dehalogenase is modeled to cleave carbon–fluorine bonds in water at ambient temperature.
| Marketpublished estimate, see source | $2.8B PFAS treatment (2025, Grand View Research) |
|---|---|
| Conditions | 20–30 °C, ambient 1 atm (design target) |
| Active site | Five active-site residues modeled; the Asp348–Arg346 contact holds only in a 400-residue crop (10.5 Å apart in the full-length model) |
Development stages
Every molecule above is labeled honestly with how far it has progressed, from an initial computer match to a physically manufactured peptide, separately from its patent filing status.
- Candidate
- Found by the screening pipeline, with a predicted structure and active-site motif. Not yet biophysically scored or simulated.
- Scored and simulated
- Passes full-length biophysical scoring and holds its fold in explicit-solvent molecular dynamics. No wet-lab assay yet.
- CRO Synthesis Queued
- Codon-optimized construct designed for a target host, ready for CRO synthesis on option execution.
- Synthesized
- Synthesized by a commercial peptide vendor, with identity and purity confirmed by HPLC and mass spectrometry. No wet-lab activity assay yet.
Why we mine extreme environments
The chemical reactions industry needs most already occur in nature; they simply evolved outside standard laboratory organisms.
Lab organisms hit a physical ceiling
Most industrial biology starts with gentle laboratory hosts like E. coli or baker’s yeast. Directed evolution can tune their enzymes, but they never evolved to survive boiling acid, concentrated salt brines, sub-zero ice, or carbon–fluorine bonds.
Purely generative AI designs often fail in cells
Generative models can propose protein backbones that look plausible on screen but have never survived inside a living cell. When expressed in a production host, many aggregate into insoluble inclusion bodies, stall secretion, or unfold under process heat.
Extreme habitats already ran the selection
Microbes in hydrothermal vents, deep-sea trenches, glaciers, and contaminated soils spent billions of years evolving durable catalysts. We recover those wild genes from public sequence archives and stress-test their 3D structures in simulated water before synthesis.
How it works
Three computational stages turn raw environmental DNA into a synthesis-ready protein construct.
Search environmental metagenomes
Researchers worldwide sequence microbial DNA from ocean trenches, glaciers, hot springs, and industrial soils and deposit those environmental genomes in public archives. Our software streams billions of those sequences to identify enzymes evolved for harsh chemistry.
Predict 3D structure & check active-site geometry
A candidate only works if it folds into the exact 3D geometry required for catalysis or binding. Structure predictors fold millions of full-length sequences in 3D, and geometric filters measure heavy-atom distances across each active pocket and metal-binding site.
Simulate stability in explicit water & heat
3D structural alignment uncovers distant natural homologs sharing less than 15% sequence identity with known enzymes. All-atom explicit-water simulations then test whether top candidates hold their fold and active-site contacts at target operating temperature.
Active discovery portfolio
64 active discovery programs across water & soil cleanup, cold-chain & climate, plastic recycling, critical minerals, and animal-free biomaterials.
Environmental remediation
Enzymes and metal-binding proteins designed to break down PFAS “forever chemicals” at room temperature, neutralize agricultural pesticides and flame retardants, and capture toxic heavy metals.
Climate & phase change
Proteins that protect thawed cells from ice damage, trigger controlled freezing for pharmaceutical freeze-drying and food cold storage, capture industrial CO2 in alkaline liquids, and break down methane.
Circular polymers
Multi-site enzymes designed to unzip PET bottles and polyester fibers in warm water, alongside candidates targeting polyurethane foams, nylon plastics, and vulcanized tire rubber.
Cellular ag, minerals & biomaterials
Animal-free cell-attachment proteins replacing cow serum, selective cages for recovering rare-earth and lithium metals, underwater bio-adhesives, and compact gene-editing enzymes.