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Literature summary for 2.4.1.162 extracted from

  • Gabrielczyk, J.; Kluitmann, J.; Dammeyer, T.; Joerdening, H.J.
    Effects of ionic strength on inclusion body refolding at high concentration (2017), Protein Expr. Purif., 130, 100-106 .
    View publication on PubMed

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
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-
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Bacillus subtilis NCIMB 11871
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Purification (Commentary)

Purification (Comment) Organism
recombinant 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, 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 Bacillus subtilis

Subunits

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

Synonyms

Synonyms Comment Organism
fructosyltransferase
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Bacillus subtilis
FTF
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Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Bacillus subtilis