重组毕赤酵母 α-葡萄糖苷酶的表达、纯化与性质鉴定。
Expression, purification and characterization of recombinant α-glucosidase in Pichia pastoris.
机构信息
Insititute of Light Industry and Food Engineering, Guang Xi University, Nanning 530005, P.R.China.
出版信息
Folia Microbiol (Praha). 2010 Nov;55(6):582-7. doi: 10.1007/s12223-010-0093-7. Epub 2011 Jan 21.
An expression plasmid containing the agdA gene encoding Aspergillus oryzae ZL-1 α-glucosidase was constructed and expressed in Pichia pastoris X-33. The molar mass of the purified protein was estimated by SDS-PAGE. HPLC analysis showed that the purified enzyme has a transglucosylating activity with maltose as substrate. The main component of the enzyme products was panose, while amounts of isomaltose and isomaltotriose were very low or absent. pH 5.2 and temperature of 37 °C were optimum for enzyme activity.
构建了含有 Aspergillus oryzae ZL-1α-葡萄糖苷酶编码基因 agdA 的表达质粒，并在 Pichia pastoris X-33 中表达。通过 SDS-PAGE 估计了纯化蛋白的摩尔质量。HPLC 分析表明，该纯化酶具有以麦芽糖为底物的转葡糖苷活性。酶产物的主要成分是潘糖，而异麦芽糖和异麦芽三糖的含量很低或不存在。酶活性的最适 pH 为 5.2，温度为 37°C。
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