Dr. Musa Mohammed Musa

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Professor, Chairman of the Chemistry Department

The research in Dr. Musa M. Musa’s laboratory focuses on developing innovative biocatalytic strategies for producing highly pure chiral molecules, key building blocks in pharmaceuticals, fine chemicals, and advanced materials.

📍 Bldg. 4-145 | Bldg. 4-225

☎ (+966) 13 860 2231 / 7343

✉ musam@kfupm.edu.sa

🔗 ORCID: 0000-0001-8191-6077

🔗 Scopus: 15760274100

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Research Area

⬡ Asymmetric Synthesis
⬡ Biocatalysis
⬡ Bioorganic Chemistry
⬡ Enzyme Encapsulation

Deracemization of Alcohols

The group designs enzyme-driven deracemization and stereoinversion processes, enabling the conversion of racemic mixtures into single, high-value enantiomers using environmentally friendly methods. The lab also explores one-pot and multi-enzyme cascade reactions, where engineered enzymes work sequentially or concurrently to carry out oxidation–reduction cycles with exceptional selectivity. These efforts have led to new concepts in cyclic deracemization, stereoinversion, and tandem enzymatic transformations, using orthogonal cofactor systems and enzyme stabilization techniques to enhance efficiency and operational simplicity.

Overall, Dr. Musa’s research advances the field of sustainable biocatalysis, demonstrating how engineered enzymes can replace traditional chemical methods to deliver cleaner, more efficient, and highly selective synthetic routes.

Tuning the Substrate Scope and Stereopreference of Alcohol Dehydrogenases

Our research focuses on engineering alcohol dehydrogenases (ADHs) to expand their substrate scope and precisely control stereopreference and stereoselectivity in the asymmetric reduction of ketones. By modifying key active-site residues in Thermoanaerobaccter pseudethanolicus secondary ADH (TeSADH), we have created enzyme variants that switch between Prelog and anti-Prelog selectivity, enabling the production of either enantiomer of valuable chiral alcohols.

These engineered mutants show broadened substrate acceptance, including halogenated and sterically demanding ketones, and allow efficient routes to optically pure alcohols and halohydrins important in pharmaceutical and fine-chemical synthesis. The ability to generate enantiocomplementary mutants also opens the door to advanced biocatalytic strategies such as dynamic kinetic resolution, stereoinversion, and cyclic deracemization.

Overall, this work demonstrates how targeted ADH engineering can create highly selective, versatile biocatalysts for greener and more efficient production of chiral building blocks.

Enzyme Encapsulation

Enzyme encapsulation enhances their stability, solvent tolerance, and reusability. This strategy enables efficient asymmetric reductions in organic media, granting access to hydrophobic, water-insoluble substrates and allowing higher substrate concentrations, an advantage for large-scale synthesis. We employ encapsulated enzymes to increase their compatibility with other biocatalysts, enabling multi-enzyme cascade reactions.

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