Enzyan

Our Approach

Being chemists by training, we consider enzymes as highly precise and tunable biocatalysts. Our approach usually follows a “retrobiosynthetic” logic that starts from a target molecule or target activity and focuses on how to use biocatalysts to arrive there. At Enzyan we combine this “synthetic chemist perspective” with a solid understanding of the underlying enzymatic reaction mechanisms and our expertise in enzymology, microbiology and molecular biology.

1

We are particularly intrigued by the compatibility of biocatalysts with each other to carry out several reactions in parallel – something that is rarely the case for chemical reagents in traditional chemical synthesis. Together with reactions that are not achievable through traditional synthetic chemistry this enables us to design and access completely new, innovative process concepts.

2

For the development of such biocatalytic cascades we can nowadays choose from an ever growing variety of well-characterized and robust biocatalysts or discover new activity in unexplored sequence space. We carefully select, mix and match these biocatalysts based on their reported activity, expected substrate promiscuities or mechanistic rationales to attain the desired activity or conversion to a target molecule.

3

With a working proof-of-concept in hand we use state-of-the-art enzyme engineering methodologies to improve the stability and activity of individual biocatalysts and adapt them to common operational conditions. To optimize the mass flux through our cascade it is crucial to balance activities of individual biocatalysts, which can be influenced by manifold reaction parameters. We address this reaction engineering task with an iterative algorithm-supported approach that allows us to arrive at optimal performance with minimal experimental effort.

4

After optimization on analytical scale (<1 mL) we take our process to the next level and demonstrate it on a preparative scale. This also enables us to investigate workup procedures and isolate the target product for characterization.

Our Experience = Your Possibilities

P450s/Peroxygenases

Ref 1  |   Ref 2
.

α-Oxoglutarate dependent dioxygenases (2OGDs)

Alcohol oxidases

Ref 4  |   Ref 5  |   Ref 6
.

Amino acid deaminases

Amino acid dehydrogenases

Confidential or unpublished data.
.

Reductive aminases (RedAm), Imine reductases (IRED)

Ref 9  |   Ref 10
.

Methyltransferases (MTs)

Ref 10  |   Ref 11
.

Carboxylic acid reductases (CARs)

Confidential or unpublished data.
.

Monoamine oxidases (MAOs)

Transaminases (TA)

Ref 9  |   Ref 13  |   Ref 14
.

Tyrosine-phenol lyases (TPL)

Tyrosine-ammonia lyases

Hydratases

Aldolases

Ref 7  |   Ref 17
.

Laccases

Hydroxynitrile lyases (HNL)

ATP-dependent ligases

Confidential or unpublished data.
.

Phenolic- and acrylic acid (de)carboxylases

Fatty acid photo-decarboxylases (FAP)

Ref 21  |   Ref 22
.

Ketoacid decarboxylases

Confidential or unpublished data.
.

Thiolases

Confidential or unpublished data.
.

Carboligases

Confidential or unpublished data.
.

Alcohol dehydrogenases

Ref 23  |   Ref 24
.

Halohydrin dehalogenases

Confidential or unpublished data.
.

Epoxidases

Confidential or unpublished data.
.

Prenyltransferases

Confidential or unpublished data.
.

Ene-Reductases

Confidential or unpublished data.
.

Phosphatases/Kinases

Confidential or unpublished data.

P450s/Peroxygenases

Ref 1  |   Ref 2
.

α-Oxoglutarate dependent dioxygenases (2OGDs)

Alcohol oxidases

Ref 4  |   Ref 5  |   Ref 6
.

Amino acid deaminases

Amino acid dehydrogenases

Confidential or unpublished data.
.

Reductive aminases (RedAm), Imine reductases (IRED)

Ref 9  |   Ref 10
.

Methyltransferases (MTs)

Ref 10  |   Ref 11
.

Carboxylic acid reductases (CARs)

Confidential or unpublished data.
.

Monoamine oxidases (MAOs)

Transaminases (TA)

Ref 9  |   Ref 13  |   Ref 14
.

Tyrosine-phenol lyases (TPL)

Tyrosine-ammonia lyases

Hydratases

Aldolases

Ref 7  |   Ref 17
.

Laccases

Hydroxynitrile lyases (HNL)

ATP-dependent ligases

Confidential or unpublished data.
.

Phenolic- and acrylic acid (de)carboxylases

Fatty acid photo-decarboxylases (FAP)

Ref 21  |   Ref 22
.

Ketoacid decarboxylases

Confidential or unpublished data.
.

Thiolases

Confidential or unpublished data.
.

Carboligases

Confidential or unpublished data.
.

Alcohol dehydrogenases

Ref 23  |   Ref 24
.

Halohydrin dehalogenases

Confidential or unpublished data.
.

Epoxidases

Confidential or unpublished data.
.

Prenyltransferases

Confidential or unpublished data.
.

Ene-Reductases

Confidential or unpublished data.
.

Phosphatases/Kinases

Confidential or unpublished data.
.

Industries & Applications

Pharmaceutical Industry

  • High stereoselectivity is crucial for making single-enantiomer drugs.
  • Mild conditions preserve sensitive functional groups.
  • Enzymes reduce the need for protecting groups and can cut short synthetic routes.

Agrochemical Industry

  • Many agrochemicals are chiral, and enzymes provide the required selectivity.
  • Eco-friendly processes support green agriculture initiatives.
  • Reduces byproducts and potential environmental hazards.

Cosmetics & Personal Care

  • Consumer push for “green beauty” and biodegradable ingredients.
  • Enzymes can customize natural oils and esters under mild conditions.

Biofuels & Biorefining

  • Breaks down tough plant biomass (lignocellulose) into fermentable sugars.
  • Enzymes help lower the energy input and increase yield in second-gen biofuels.

Fine & Specialty Chemicals

  • Enzymes make complex molecules with fewer steps and cleaner reactions.
  • Great for high-value, low-volume chemicals where purity and selectivity are vital.