[Purification and some properties of Clostridium thermocellum endoglucanase, formed by a recombinant Escherichia coli strain].
The endoglucanase (EG5) has been isolated from the recombinant strain of E. coli TG1 carrying a plasmid with C. thermocellum F7 chromosomal DNA insertion. Using high performance ion-exchange chromatography and chromatofocusing, the enzyme was 98-fold purified with a 27% yield. The enzyme has a molecular mass of 35 kDa (SDS-PAGE data) and is represented by three isoforms with pI 4.4-4.8 (isoelectrofocusing data). The activity of EG5 was determined by chromatography on carboxymethylcellulose, amorphous cellulose, xylan, lichenan and avicel. The optimal conditions for these substrates hydrolysis are: pH 6.0-6.5, 80 degrees C (60 degrees C for avicel).
Mosolova
T P
TP
Kaliuzhnyĭ
S V
SV
Velikodvorskaia
G A
GA
D002480:Cellulase / Q000302:isolation & purification* / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003013:Clostridium / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics*; D007525:Isoelectric Focusing; D010957:Plasmids; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism
D011994:Recombinant Proteins; D002480:Cellulase