کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10233426 | 42752 | 2005 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Expression and overproduction of recombinant penicillin G acylase from Kluyvera citrophila in Escherichia coli
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Heterologous production of Kluyvera citrophila penicillin G acyalse (KcPGA) was optimized in Escherichia coli (E. coli). Several factors, including the effect of different medium and culture performance were identified to be crucial for the enzyme overproduction. The KcPGA yield was significantly and conveniently increased by more than 2.4-fold in TB medium compared to that in LB medium, which need inducing by isopropylthio-beta-d-galactoside (IPTG). The results shown the lower temperature (28 °C) was more feasible for the overproduction of KcPGA compared to the higher temperature (37 °C). The highest enzyme activity was obtained at 28 °C in TB medium only when culture pH was closed to its original pH value and the basic condition was more optimal for the production of KcPGA than that of acidic condition. On the other hand, the higher temperature (37 °C) culture condition resulted in poor enzyme activity although the optimum growth temperature for most of the E. coli strains is approximately 37 °C. It was possible due to the limitation by translation or posttranslational steps of the heterologous production of KcPGA in E. coli. The results suggest that culture temperature and pH should be precisely controlled for overproduction of KcPGA in E. coli.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Enzyme and Microbial Technology - Volume 37, Issue 2, 1 July 2005, Pages 233-237
Journal: Enzyme and Microbial Technology - Volume 37, Issue 2, 1 July 2005, Pages 233-237
نویسندگان
Yong Wen, Meiqing Feng, Zhongyi Yuan, Pei Zhou,