嗜冷基因在嗜温宿主中的表达：重组α-淀粉酶折叠状态的评估
Expression of psychrophilic genes in mesophilic hosts: assessment of the folding state of a recombinant alpha-amylase.
作者信息
Feller G, Le Bussy O, Gerday C
机构信息
Laboratory of Biochemistry, University of Liège, Liège-Sart Tilman, Belgium.
出版信息
Appl Environ Microbiol. 1998 Mar;64(3):1163-5. doi: 10.1128/AEM.64.3.1163-1165.1998.
Abstract
Alpha-Amylase from the antarctic psychrophile Altermonas haloplanktis is synthesized at 0 +/- 2 degrees C by the wild strain. This heat-labile alpha-amylase folds correctly when overexpressed in Escherichia coli, providing the culture temperature is sufficiently low to avoid irreversible denaturation. In the described expression system, a compromise between enzyme stability and E. coli growth rate is reached at 18 degrees C.
摘要
来自南极嗜冷菌嗜盐浮游交替单胞菌的α-淀粉酶由野生菌株在0±2摄氏度下合成。这种热不稳定的α-淀粉酶在大肠杆菌中过表达时能正确折叠，前提是培养温度足够低以避免不可逆变性。在所描述的表达系统中，在18摄氏度时实现了酶稳定性和大肠杆菌生长速率之间的折衷。
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