Fakruddin Md, Mohammad Mazumdar Reaz, Bin Mannan Khanjada Shahnewaj, Chowdhury Abhijit, Hossain Md Nur
Industrial Microbiology Laboratory, Institute of Food Science and Technology (IFST), Bangladesh Council of Scientific and Industrial Research (BCSIR), Dhaka 1205, Bangladesh.
BCSIR Laboratories, Chittagong, Chittagong 4220, Bangladesh.
ISRN Biotechnol. 2012 Aug 13;2013:590587. doi: 10.5402/2013/590587. eCollection 2013.
E. coli is the most frequently used host for production of enzymes and other proteins by recombinant DNA technology. E. coli is preferable for its relative simplicity, inexpensive and fast high-density cultivation, well-known genetics, and large number of compatible molecular tools available. Despite all these advantages, expression and production of recombinant enzymes are not always successful and often result in insoluble and nonfunctional proteins. There are many factors that affect the success of cloning, expression, and mass production of enzymes by recombinant E. coli. In this paper, these critical factors and approaches to overcome these obstacles are summarized focusing controlled expression of target protein/enzyme in an unmodified form at industrial level.
大肠杆菌是通过重组DNA技术生产酶和其他蛋白质时最常用的宿主。由于其相对简单、廉价且快速的高密度培养、广为人知的遗传学以及大量可用的兼容分子工具,大肠杆菌是比较理想的选择。尽管有所有这些优点,但重组酶的表达和生产并不总是成功的,并且常常导致产生不溶性和无功能的蛋白质。有许多因素会影响通过重组大肠杆菌克隆、表达和大规模生产酶的成功与否。本文总结了这些关键因素以及克服这些障碍的方法,重点是在工业水平上以未修饰的形式可控表达目标蛋白质/酶。