![]() ![]() However, the fine examination of physiological responses to protein production in bacteria and other microorganisms, has revealed that chaperone co-production, as a quality-addressed strategy, might eventually show undesirable side effects regarding protein yield and quality (Table 1). coli), most of these approaches have involved the two main cytosolic chaperones, namely DnaK and GroEL, as well as some of their co-chaperones. Therefore, several individual chaperones or chaperone sets have been selected for overproduction along with the target recombinant protein. Under the high substrate load context of recombinant cells, chaperones, main players in the quality control system, might be over-titrated and therefore their protein targets excluded from folding pathways leading to the native conformation, accumulating as refractile particles called inclusion bodies (IBs). by decreasing temperature), reducing recombinant gene dosage or the strength of the promoter, or supplying additional amounts of host chaperones, as they are seen as limiting during the overproduction of misfolding-prone protein species. Traditionally, gaining solubility has been approached by tuning-down the production rate (e.g. Although what protein quality means might be highly controversial, it is in general assumed that the soluble protein version, despite the potential occurrence of soluble aggregates and the presence of functional protein species in protein aggregates, is the most desirable form of the final product of a protein production process. Recombinant protein misfolding and the triggering of the consequent cell responses are both general events among microbial cell factories. Poor product quality is a common event in the biological synthesis of target proteins and a major cause for recombinant enzymes and pharmaceuticals to be excluded from the market. ![]()
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