摘要
利用甲醇诱导重组Pichia pastoris在发酵罐中表达几丁质酶,在发酵过程中根据溶氧变化控制甲醇流加速度。结果显示,蛋白表达量随菌体密度的增加而增加,酶活最高达56 U/ml。该几丁质酶具有良好的耐热性和pH适应性,在pH 2.0和pH 5.0有2个最适反应pH;在pH 3.0稳定性最好;40℃为其最适反应温度;在60℃保温3 h仍保持81%的酶活性;该几丁质酶对病原菌生长有一定程度抑制作用。
The rice chitinase was expressed in the fermentor by the recombinant Pichia pastoris with methanol induction. During the period of fermentation, the methanol feeding rate was varied with the change of DO level. The results indicated that the higher fmal protein level obtained because of the increased cell density. The highest chitinase activity was 56 U/ml. The enzyme was most active at pH 2.0, pH 5.0 and 40℃, and most stable at pH 3.0. The enzyme had good therrmstablilty, which still retained 81% of its activity after being preserved at 60 ℃ for 3 h. The pathogen could be inhibited by the enzyme to a certain extent.
出处
《安徽农业科学》
CAS
北大核心
2007年第7期2018-2020,共3页
Journal of Anhui Agricultural Sciences
基金
天津市应用基础研究计划面上项目(06YFJC1200)
关键词
毕赤酵母
几丁质酶
发酵
酶学性质
Pichiapastoris
Chitinase
Fermentation
Enzyme characteristic
