Literature summary for 2.4.1.162 extracted from

Gabrielczyk, J.; Joerdening, H.J.
Ion exchange resins as additives for efficient protein refolding by dialysis (2017), Protein Expr. Purif., 133, 35-40 .

Search for more literature for 2.4.1.162

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of C-terminally Strep-tagged enzyme in Escherichia coli strain BL21(DE3) Rosetta in inclusion bodies	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-
Bacillus subtilis NCIMB 11871	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant reatures soluble C-terminally Strep-tagged enzyme from Escherichia coli strain BL21(DE3) Rosetta inclusion bodies by Strep-Tactin affinity chromatography and dialysis	Bacillus subtilis

Renatured (Commentary)

Renatured (Comment)	Organism
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	Bacillus subtilis

Renatured (Comment)

Organism

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

Bacillus subtilis

Subunits

Subunits	Comment	Organism
monomer	1 * 51620, sequence calculation and SDS-PAGE	Bacillus subtilis

Synonyms

Synonyms	Comment	Organism
fructosyltransferase	-	Bacillus subtilis
FTF	-	Bacillus subtilis

pI Value

Organism	Comment	pI Value Maximum	pI Value
Bacillus subtilis	sequence calculation	-	5.75