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This research demonstrates that lipases from solid-state fermentation of Pycnoporus sanguineus effectively catalyze esterification and kinetic resolution of sec-alcohols.
Lipases are widely used as biocatalysts in synthetic applications because of their high chemo-, regio-, and enantioselectivities, which play key roles in the synthesis of esters and the resolution of racemates. These biocatalytic steps are essential for the production of various products, including cosmetic ingredients, building blocks in the pharmaceutical and agrochemical industries. In this study, we produced lipases through solid-state fermentation of agricultural by-products and domestic wastes using the fungus Pycnoporus sanguineus. After fermentation, the dried solids containing lipases from P. sanguineus exhibited high catalytic activity. Lipase production was achieved via solid-state fermentation using a substrate composed of wheat bran and sugarcane bagasse supplemented with either residual frying oil or urea, resulting in an enzymatic activity of 24 U mL−1 after 96 h. The resulting P. sanguineus fermentation solids (PSFS) efficiently catalyzed the esterification of capric acid with ethanol, achieving 95% ester conversion within 28 h. Additionally, PSFS proved to be effective in the kinetic resolution of (RS)-1-phenyl-1-ethanol via transesterification with various acyl donors, selectively forming the (R)-enantiomer. This process yielded a 16% conversion to (R)-1-phenylethyl propionate and an enantiomeric ratio (E) exceeding 200 after 72 h. These results demonstrate the potential of PSFS for applications in ester synthesis and resolution of enantiomerically pure sec-alcohols.
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Ferreira et al. (2025) studied this question.
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