Enzymes & Biocatalysis
Bio-catalysis has become a potent tool in green synthesis of APIs and other biological small molecules. Pharmaceutical companies are increasingly integrating this green synthesis approach with traditional medicinal chemistry, to bring resource efficiency and environmental safety in the manufacturing processes. Bio-catalysis has been proven as a substitute for conventional chemo-catalysis, providing more sustainable, safe, and efficient methods for the production of APIs and advanced pharmaceutical intermediates.
Our technology team developed highly efficient engineered enzymes for biocatalytic applications in production of pharmaceutical APIs. This was achieved through random and site-directed mutagenesis, enzyme-directed evolution, Molecular Docking and MD simulation methods, together with our microbial recombinant enzyme production platforms. We further improved the enzyme yields to competent scale and established low cost and robust commercial manufacturing process.
Our Biocatalysis enzymes
Salient features
Tailor made ENZYMES for selective, robust biocatalysts. Process oriented biocatalysts (enzymatic manufacturing of pharmaceutical small molecules). State-of-the-art process technologies (Turnkey solutions for complete process scheme of target API molecules) Our engineered microbial expression platforms ensure high quality and easy production scale-up.
Transaminase
Amine transaminases (ATA) catalyze the transfer of an amino group from a primary amine to a prochiral ketone (or aldehyde). Amine transaminases are highly enantioselective and therefore can be used for the resolution of racemic amines or the synthesis of chiral amines from inexpensive ketones. ATAs are pyridoxal-5‘-phosphate dependent enzymes and their substrate range includes alkyl and aromatic amines, amino acids, amino esters and amino alcohols. Typical amine donors are: alanine, ethylamine, 1- and 2-propylamine, 1- and 2-butylamine and others.
Alcohol dehydrogenases (ADHs, also ketoreductases, KRED) are among the most widely used biocatalysts for the industrial-scale synthesis of APIs
Nitrilase
Nitrilases catalyze the hydrolysis of nitriles to the corresponding carboxylic acids and potentially interesting catalysts for the enantioselective synthesis of carboxylic acids from readily available nitrile precursors.
It is well-known that nitrilases are rather sensitive enzymes owing to the presence of an oxygen-sensitive cysteine residue in the active site.
Lipases, catalyze the hydrolysis of water-insoluble esters such as triglycerides like triolein to diolein.
In addition, lipases also catalyze the hydrolysis of a broad range of natural and unnatural esters, while retaining high enantio- or regioselectivity. They require no cofactors and are simple to use.
This combination of broad substrate range and high selectivity makes lipases an ideal catalyst for organic synthesis.
Pharmaceutical industry use lipase mediated biocatalysis for sterio- and regio- selective catalysis.
Glucose Dehydroginase
Glucose dehydrogenases are defined as oxidoreductases that are unable to utilize oxygen as the electron acceptor and instead transfer electrons to various natural and artificial electron acceptors
The enzyme catalyzes oxidation of the first hydroxyl group of glucose, utilizing NAD+ or NADP+ as the primary electron acceptor.
Halohydrin dehalogenases convert vicinal halohydrins to an epoxide, a halide ion, and a proton.
Halohydrin dehalogenases catalytic reactions are reversible, depending on the nature of the leaving group. This enzyme catalysis can generate enantiomerically pure compounds which can be used as chiral building blocks for the syntheses of a wide range of small chemical molecules.
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