2-phenylethyl-β-D-glucopyranoside, a glycoside compound mainly found in Magnoliaceae plants, has been proved to have many biological activities, such as antioxidant, anti-inflammatory, antibacterial, antiviral, antitumor, neuroprotective and immunomodulatory effects. In the production of chemical reaction, the application range is greatly limited due to the tedious steps in the reaction process and the easy generation of chemical residues. Enzymatic synthesis of glycoside compounds has attracted wide attention in recent years because of its mild reaction conditions, high selectivity and direct use of unprotected free sugar as substrate.<br/>According to literature reports, UGT73B6, UGT72B14 and UGT85A1 can catalyze tyrosol to produce salidroside, while UGT76G1 can catalyze alcohol substrate. The structure of 2- phenylethanol is similar to that of salidroside. In order to screen out 2-phenylethyl-β-D-glucopyranoside which can catalyze 2-phenylethanol to produce 2-phenylethanol glycoside. The above four glycosyltransferase were constructed in pRSFDuet-1 vector, and <i>Escherichia coli</i> BL21(DE3) was used as the host to construct the biosynthetic pathway that catalyzed 2- phenylethanol to produce 2-phenylethyl-β-D-glucopyranoside, and the glycosyltransferases that could transform 2-phenylethanol were screened.<br/>The sequence with the highest conversion activity to 2-phenylethanol was selected as UGT85A1. UGT73B6 and UGT76G1 have very low catalytic activity for 2-phenylethanol, while UGT72B14 does not react at all. The specific enzyme activity of UGT85A1 to 2-phenylethanol as substrate reached 30 mu/mg, and the yield reached 75% when the substrate concentration was 5 mM.

Screening glycosyltransferase with 2- phenylethanol as substrate

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