Effect of Lipase Induction on Whole-cell Biocatalyst Behavior during Esculin Acylation and Structural Identification of Products
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Abstract:
A novel method to synthesize flavonoid ester was explored. Different induction media were used to culture six strains for high-yield lipase production. The whole-cell catalyst was prepared and used to catalyze the reaction of esculin and vinyl propionate with pyridine as the reaction solvent. The results indicated that two strains, Pseudomonas aeruginosa GIM 1.46 and P. stutzeri GIM 1.273, showed the ability to catalyze the propionylation of esculin, with P. stutzeri GIM 1.273 showing the highest catalytic activity. The effect of different lipase inducers on biomass and catalytic activity of the whole cells was investigated by adding soy oil, Tween 80, or glucose into the screening culture. The results showed that P. stutzeri GIM 1.273 cultivated in a medium containing soy oil exhibited the highest activity, where conversion rates for esculin propionylation reached 47.9% after 48 h. The products were purified and structurally identified using mass spectrometry (MS) and 13C-nuclear magnetic resonance (13CNMR) spectroscopy, which showed that the whole cells catalyzed the acylation of 6’-OH in esculin, the resulting product was esculin-6’-O-propionate, where the regioselectivity reached 99%.
