@article{open1221, volume = {123}, month = {November}, author = {Kamna Jhamb and Debendra K Sahoo}, note = {Copyright of this article belongs to Elsevier Science.}, title = {Production of soluble recombinant proteins in Escherichia coli: effects of process conditions and chaperone co-expression on cell growth and production of xylanase.}, publisher = {Elsevier Science}, journal = {Bioresource technology}, pages = {135--43}, year = {2012}, keywords = {Escherichia coli;Inclusion bodies;Soluble expression; Molecular chaperones, Xylanase}, url = {http://crdd.osdd.net/open/1221/}, abstract = {In this study, effects of temperature, inducer concentration, time of induction and co-expression of molecular chaperones (GroEL-GroES and DnaKJE), on cell growth and solubilization of model protein, xylanases, were investigated. The yield of soluble xylanases increased with decreasing cultivation temperature and inducer level. In addition, co-expression of DnaKJE chaperone resulted in increased soluble xylanases though the time of induction of chaperone and target protein had a bearing on this yield. A combination of chaperone co-expression and partial induction resulted in {$\sim$}40\% (in DnaKJE) and 33\% (in GroEL-GroES) of total xylanase yield in soluble fraction. However, the conditions for maximum yield of soluble r-XynB and maximum \% soluble expression of r-XynB were different. Higher expression of soluble xylanases in a scalable semi-synthetic medium showed potential of the process for soluble enzyme production.} }