Jiang Zheng-Bing, Song Hui-Ting, Ma Li-Xin
College of Life science, Hubei University, Wuhan 430062, China.
Sheng Wu Gong Cheng Xue Bao. 2003 Jan;19(1):50-5.
The endo-1,4-xylanase gene from Bacillus pumilus HB030 was cloned into the Pichia pastoris expression vector, pPIC9k, the recombinant plasmid was named pHBM220. The digested recombinant plasmid pHBM220 was transformed into Pichia pastoris KM71, GS115, SMD1168, respectively. The recombinant Pichia pastoris KM71 (pHBM220), GS115 (pHBM220), SMD1168 (pHBM220) secreted functional endo-1,4-xylanase, and the enzymatic activities reached 10.80IU/mL, 11.63IU/mL, 9.68IU/mL, respectively. The temperature and pH optimum for the recombinant xylanase were 60 degrees C and pH5.5, respectively.
将短小芽孢杆菌HB030的内切-1,4-木聚糖酶基因克隆到毕赤酵母表达载体pPIC9k中，重组质粒命名为pHBM220。将酶切后的重组质粒pHBM220分别转化到毕赤酵母KM71、GS115、SMD1168中。重组毕赤酵母KM71（pHBM220）、GS115（pHBM220）、SMD1168（pHBM220）分泌具有功能的内切-1,4-木聚糖酶，酶活性分别达到10.80IU/mL、11.63IU/mL、9.68IU/mL。重组木聚糖酶的最适温度和pH分别为60℃和pH5.5。
