2.4.1.162	recombinant C-terminally Strep-tagged enzyme from Escherichia coli strain BL21(DE3) Rosetta inclusion bodies by ion exchange chromatography and dialysis, method optimization and evaluation of renaturation, overview. Conventional anion exchangers with gel matrix structure enhance refolding performance by about 43% with final protein concentration of 9 mg/ml and yield improvement is strictly linear dependent on the mass ratio of resins to protein, purolite ion exchange resins are then employed. With the applied setup refolded protein is self-eluted from resin due to pH and salt concentration shift during dialysis. Macroporous resins and gel filtration media show a negative effect on refolding yields	
2.4.1.162	recombinant C-terminally Strep-tagged enzyme from Escherichia coli strain BL21(DE3) Rosetta inclusion bodies, method optimization and evaluation of a cost effective renaturation, detailed overview. The enzyme is solubilized from batch sample by detergent buffer containing 1 M urea, 0.1 M Tris, 25 mM deoxycholate, and 1% v/v IGEPAL CA-630. Refolding is done by batchwise or continuous exchange of dialysis buffer with cellulose membrane, over a period of 48 h and a buffer to sample volume ratio of 100:1 at 4°C, batch dialysis. Mild solubilization at low urea concentration (2 M) and high pH (pH 12) does not improve the recovery of protein from inclusion bodies. Phosphate buffers exhibit above-average activity yield of 1022 U/ml