Proteins, engineered
to endure.

We evolve proteins inside an extremophile. The ones that survive come out ready for what's next — searing heat, stomach acid, and the long road through.

01 The bottleneck

Most useful proteins
inevitably fall apart on the way.

Proteins are the working parts of biology — and they are fragile by default. Heat denatures them. Low pH unfolds them. Digestive enzymes take them apart. Whatever a protein does on a bench, it usually stops doing somewhere between processing, storage, and digestion.

Engineering around this — making a protein both active and durable — has historically taken teams years and entire platforms of infrastructure. The problem isn't creativity; it's throughput. You can design ten thousand variants in an afternoon. Testing them for real survival is where time goes to die.

Through heat sterilisation.

From pasteurisation to full retort sterilisation, our variants retain function across the thermal processing that makes food shelf-stable.

Through low pH.

Selected in an acid-tolerant host, variants emerge with folding that doesn't unravel in wet-food matrices or in the stomach.

Through digestion.

Protease resistance lets the protein survive its passage through the gut — emerging intact and still functional.

02 Our approach

We screen proteins inside
something that already lives at the edge.

Our screen runs inside a living extremophile — an organism that already tolerates the conditions we care about. Variants that can't survive simply don't make it through. The ones that do are real hits the first time you see them.

I.

Generate

Libraries of protein variants — from thousands to millions, designed against a target function.

II.

Select in vivo

The library is expressed inside our extremophile host. The environment is the selection — variants that fold and function survive; the rest don't.

III.

Discover

Hits come out already tested against the conditions they'll meet downstream. Weeks of wall-clock time, not months or years.

10k–100k
variants tested per run
2–4wk
from library to ultra-resilient leads
1
organism doing selection and expression at once

03 First application

A protein that can
live inside a finished food.

Affineo is tackling durability where it matters most. In shelf-stable ingredients, wet-format products and functional nutrition, a fragile protein simply won't work. Ours are built to last.

Early focus area

Anti-allergenic wet cat food

We are developing proteins that target Fel d 1 — the main molecule responsible for cat allergies in humans. While existing approaches break down under heat and moisture and only work in dry kibble, our proteins are built to survive retort sterilisation and remain active in wet food. Functioning seamlessly as part of the cat's normal diet, they'll require no changes to the owner's routine.

Learn more about Fel d 1 programme

04 Our team

Paris-based,
with shared roots in Cambridge.

Dariusz Czernecki
Science & Operations

Dariusz Czernecki

  • École Normale Supérieure
  • Sorbonne Université
  • Institut Pasteur
  • MRC Laboratory of Molecular Biology
LinkedIn
Maxime Crabé
Strategy & Partnerships

Maxime Crabé

  • École Polytechnique
  • University of Cambridge
  • Collège des Ingénieurs
  • Boston Consulting Group
  • Cepton Strategies
LinkedIn

05 Partners & programmes

Backed by the people
building deeptech in France.

Affineo is supported by Genopole — first through the Shaker programme, now through Gene.iO — and joins the latest Wilco One cohort for Foodtech & Agritech.

  • Genopole
    Biocluster · Évry
  • Shaker
    Pre-incubation · alumni
  • Gene.iO
    Incubation · current
  • Wilco One
    Foodtech & Agritech cohort
Affineo Affineo

Let's talk about what becomes possible when proteins actually last.

Partnerships

Food, nutrition, and companion-animal ingredient teams exploring durable protein additives.

Investors

Seed and strategic investors with conviction in platform biotech and food-grade biomanufacturing.

Reach the team contact@affineo.bio
4 rue Pierre Fontaine, 91000 Évry-Courcouronnes