[Isolation and certain properties of the thermostable endoglucanase from E. coli C600 (pKNE-102) coded by a Clostridium thermocellum gene].
A previously unknown endoglucanase encoded by the C. thermocellum gene was isolated from the recombinant strain of E. coli (pKNE-102). The purification procedure included ammonium sulfate precipitation, heat treatment, chromatography on a polyvinyl matrix (Toyopearl HW-50F) and chromatofocusing on a high performance Mono P HR 5/20 column. Sodium dodecyl sulfate electrophoresis analysis of the Toyopearl HW-50F effluent revealed two protein bands with Mr of 41 kDa and 42 kDa. These protein components differed also by their pI values (4.45, and 4.40, respectively) and could be separated by chromatofocusing. Both components were found to be active and exhibited similar enzymatic properties as well as high thermal stability.
Golovchenko
N P
NP
Kataeva
I A
IA
Bukhtiiarova
M G
MG
Aminov
R I
RI
Tsoĭ
T V
TV
Akimenko
V K
VK
Boronin
A M
AM
D002480:Cellulase / Q000302:isolation & purification* / Q000378:metabolism; D002853:Chromatography, Liquid; D003013:Clostridium / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology*; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D005798:Genes, Bacterial; D006358:Hot Temperature; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism
D011994:Recombinant Proteins; D002480:Cellulase
Vydelenie i nekotorye svoĭstva termostabil'noĭ éndogliukanazy iz E. coli C 600 (pKNE-102), kodiruemoĭ genom Clostridium thermocellum.