Preparation of Naringin Ester by Enzymatic Transesterification and Its Inhibition of HepG2 Cell Proliferative Activity
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Abstract:
In this paper, the immobilized lipase IMTL was used to catalyze the transesterification of naringin under non-aqueous conditions to produce a series of naringin esters with different fatty acid chain length. The immobilized lipase IMTL enzyme showed high catalytic activity towards the reaction, with substrate conversion ratios being above 90%. In a 4 mL tert-amyl alcohol system, 50 mg of lipase IMTL, naringin: acyl donor=1:20, and the reaction was performed at 50 ℃ for 3 hours, and the regioselectivity was above 99%. After the naringin esters were analyzed and identified by HPLC, mass spectrometry, and nuclear magnetic resonance, the acylated products were naringin-6’’-o-ester. It was found that the ClogP values of naringin esters increased with the increase of the chain length. Among them naringin myristate ClogP value was 6.50. The results of HepG2 cell inhibition experiments showed that the inhibitory activity of naringin esters on HepG2 cell proliferation was closely related to their lipophilicities. Compared with naringin, naringin esters had a better inhibitory effect on HepG2 cell. Naringin myristate with long-chain fatty acid had better fat solubility and stronger inhibitory effect on HepG2 cell proliferation (2.28%). The enzymatically synthesized esters may have a broader application prospect than naringin.
