Enzymatic Preparation of Puerarin Ester Derivatives
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Abstract:
In this paper, the catalytic efficiency of different kinds of enzymes on the acylation reaction of puerarin was studied in non-aqueous phase. Among 8 kinds of enzymes, immobilized lipases Novozym 435, Lipozyme IMTL and Lipozyme IMRM could efficiently catalyze the acylation reaction of puerarin and conversion rate was as high as 98%, but the activity and efficiency of other free lipases catalyzed the acylation of puerarin were very low. Under the same conditions, the conversion rate of puerarin catalyzed by porcine lipase was about 67%, pancreatic lipase and CRL lipase showed low catalytic activity, and peptidase and protease did not exhibit catalytic activity. And Novozym 435 showed the highest catalytic activity. Using Novozym 435 as catalyst, the optimum reaction medium, dosage of lipase catalysts, mole ratio of substrates, initial water content and reaction time were determined as THF, 1:30, 2 mg/mL, 0 and 6 h, respectively. Under the above reaction conditions, conversion of puerarin reached 99.5%. The products were purified and structurally identified using HPLC, mass spectrometry (MS) and fourier transform infrared spectroscopy (FT-IR) which showed that the lipase catalyzed the acylation of puerarin, the resulting product was puerarin propionate monoester, where the regioselectivity reached 98%.
