Enantioselective transesterification using lipase-displaying yeast whole-cell biocatalyst

Area of Science:

• Biocatalysis
• Organic Chemistry
• Biotechnology

Background:

• Enantioselective synthesis is crucial for chiral building blocks.
• Lipase-based biocatalysis offers a green alternative for chiral resolutions.
• Whole-cell biocatalysts can simplify enzyme immobilization and handling.

Purpose of the Study:

• To develop an enantioselective transesterification using a lipase-displaying yeast whole cell biocatalyst.
• To optimize the optical resolution of (RS)-1-phenylethanol in non-aqueous organic solvents.
• To evaluate the stability and activity of the biocatalyst in various organic media.

Main Methods:

• Construction of a recombinant yeast whole cell biocatalyst displaying Rhizopus oryzae lipase.
• Enantioselective transesterification of (RS)-1-phenylethanol with vinyl acetate in organic solvents (hexane, heptane, cyclohexane, octane).
• Optimization of reaction conditions, including biocatalyst loading (10 mg/ml) and use of molecular sieves 4A.

Main Results:

• The lipase-displaying yeast retained activity in tested non-aqueous solvents.
• High yield (97.3%) and enantiomeric excess (93.3% ee) of (R)-1-phenylethyl acetate were achieved within 36 hours.
• Molecular sieves 4A were essential for efficient product formation.

Conclusions:

• The developed lipase-displaying yeast whole cell biocatalyst is effective for enantioselective transesterification in non-aqueous organic solvents.
• This biocatalyst demonstrates significant potential for the industrial-scale optical resolution of chiral alcohols.
• The use of whole-cell biocatalysts offers a practical and efficient approach for bioconversion processes.