The advancements in biotechnology over time have led to an increase in the demand of pure, soluble and functionally active proteins. Recombinant protein production has thus been employed to obtain high expression of purified proteins in bulk. E. coli is considered as the most desirable host for recombinant protein production due to its inexpensive and fast cultivation, simple nutritional requirements and known genetics. Despite all these benefits, recombinant protein production often comes with drawbacks, such as, the most common being the formation of inclusion bodies due to improper protein folding. Consequently, this can lead to the loss of the structure-function relationship of a protein. Apart from various strategies, one major strategy to resolve this issue is the use of molecular chaperones that act as folding modulators for proteins. Molecular chaperones assist newly synthesized, aggregated or misfolded proteins to fold into their native conformations. Chaperones have been widely used to improve the expression of various proteins which are otherwise difficult to produce in E. coli. Here, we discuss the structure, function, and role of major E. coli molecular chaperones in recombinant technology such as trigger factor, GroEL, DnaK and ClpB.

随着时间的推移，生物技术的进步导致对纯、可溶性和功能活性蛋白质的需求增加。因此，重组蛋白生产已被用于批量获得纯化蛋白的高表达。大肠杆菌由于其廉价和快速的培养、简单的营养需求和已知的遗传学，被认为是重组蛋白生产最理想的宿主。尽管有所有这些好处，重组蛋白的生产通常也有缺点，例如，最常见的是由于蛋白质折叠不当而形成包涵体。因此，这会导致蛋白质结构-功能关系的丧失。除了各种策略之外，解决这个问题的一个主要策略是使用分子伴侣作为蛋白质的折叠调节剂。分子伴侣帮助新合成、聚集或错误折叠的蛋白质折叠成它们的天然构象。分子伴侣已被广泛用于改善各种蛋白质的表达，否则这些蛋白质很难在大肠杆菌。在这里，我们讨论了主要大肠杆菌分子伴侣在重组技术中的结构、功能和作用，例如触发因子、GroEL、DnaK 和 ClpB。