将含重组质粒pET28b-ValG 在BL21（DE3）宿主菌中成功表达，以镍柱亲和层析、超滤脱盐及真空冷冻干燥结晶获得糖基转移酶并初步研究酶学性质。在10～40 °C 或pH 5～11 下，该酶还能保持较好的稳定性，且最适反应温度及pH 分别为30 °C 与8.0。1 mmol/L 金属离子Ca2+、Mg2+、Mn2+、Co2+对酶反应有着显著的促进作用， 而Cu2+、Zn2+对酶反应有强烈的抑制效果。当酶反应进程中酶活达到最大时，底物及产物的最适浓度分别为8 μmol/L 与2 μmol/L。以底物井冈羟胺A 足量为前提， 双倒数作图法表明KmB为35.275 μmol/L，Vm为0.153 μmol/(L·min)，酶对井冈羟胺A 的亲和力较尿苷二磷酸葡糖（UDPG）好，因此在全细胞酶催化过程中对提高UDPG 供应量的研究是有必要的。

The recombinant plasmid pET28b -ValG was functionally expressed in E.coli BL21（DE3） and the overexpressed glycosyltransferase was purified sequentially by nickel affinity chromatography, ultra-filtration desalination and freeze-drying. Then the purified enzyme was characterized and it showed good stability at 10-40 °C and pH 5-11. The optimum reaction temperature and pH were 30 °C and 8.0, respectively. The metal ions, such as Ca2+, Mg2+, Mn2+ and Co2+, activated the enzyme activity, while Cu2+ and Zn2+ inhibited the enzyme activity instead. The maximum enzyme activity was obtained at substrate and product concentrations of 8 μmol/L and 2 μmol/L, respectively. When sufficient validoxylamine A was added as substrate, the Lineweaver-Burk plot showed that the KmB and Vm were 35.275 μmol/L and 0.153 μmol/(L·min), respectively. The affinity of validoxylamine A was much better than that of the uridine diphosphate glucose (UDPG) to the glycosyltransferase, which made it necessary to study the supply of UDPG in the process of the whole-cell catalysis.