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乙醛脱氢酶2基因在毕赤酵母中的表达和分离纯化
引用本文:陈瑞,方剑,王静涵. 乙醛脱氢酶2基因在毕赤酵母中的表达和分离纯化[J]. 生物加工过程, 2013, 0(6): 34-37
作者姓名:陈瑞  方剑  王静涵
作者单位:[1]皖西学院生物与制药工程学院,六安237012 [2]皖西学院安徽省植物生物技术实验实训中心,六安237012
基金项目:大学生创新创业计划项目(201210376007); 六安市定向委托皖西学院市级研究项目(2012LW001)
摘    要:将乙醛脱氢酶2(ALDH2)基因整合到质粒pPIC9K上,构建重组表达载体pPIC9K-coALDH2,用电转导将表达质粒pPIC9K-coALDH2转化至毕赤酵母GS115中,在毕赤酵母中表达经密码子改造的ALDH2。结果表明:重组基因工程菌GS115(pPIC9K-coALDH2)发酵液中蛋白质量浓度为8.40 mg/L,1 mL发酵液中酶活为11.35 mU。

关 键 词:乙醛脱氢酶  GS115  表达

Expression of acetaldehyde dehydrogenase 2 gene in Pichia pastoris
CHEN Rui,FANG Jian,WANG Jinghan. Expression of acetaldehyde dehydrogenase 2 gene in Pichia pastoris[J]. Chinese Journal of Bioprocess Engineering, 2013, 0(6): 34-37
Authors:CHEN Rui  FANG Jian  WANG Jinghan
Affiliation:1. College of Biology and Pharmaceutical Engineering, West Anhui University, Lu'an 237012, China ; 2. Experiment and Training Center of Plant Biotechnology of Anhui Province, West Anhui University, Lu'an 237012, China)
Abstract:To obtain acetaldehyde dehydrogenase 2 (ALDH2), the pPIC9K-ALDH2 was linearized and transformed by electroporation into Pichia pastoris GSll5, and the new engineering bacteria GSll5 (pPIC9K-colALDH) for overexpressing ALDH2 was obtained. The results showed that the content of target protein was 8.40 mg./L and the enzymatic activities in culture recombinant Pichia strains reached 11.35 mU/mL, and it was higher than that in extracellular expression.
Keywords:acetaldehyde dehydrogenase  GS115  express
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