Purification and characterization of endoglucanase Ss from Clostridium thermocellum
نویسندگان
چکیده
منابع مشابه
Clostridium thermocellum Endoglucanase Produced in Escherichia coli
was purified from extracts of plasmid-bearing E. coli cells by heat treatment and chromatography on DEAE-Trisacryl. It was characterized as a thermophilic endo-4-1,4-glucanase, the properties of which closely resemble those of endoglucanase A previously isolated from C. thermocellum supernatants. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis the enzyme purified from E. coli exhib...
متن کاملCenC, a multidomain thermostable GH9 processive endoglucanase from Clostridium thermocellum: cloning, characterization and saccharification studies.
The growing demands of bioenergy has led to the emphasis on novel cellulases to improve efficiency of biodegradation process of plant biomass. Therefore, a thermostable cellulolytic gene (CenC) with 3675 bp was cloned from Clostridium thermocellum and over-expressed in Escherichia coli strain BL21 CodonPlus. It was attested that CenC belongs to glycoside hydrolase family 9 (GH9) with four bindi...
متن کاملTranscription of Clostridium thermocellum endoglucanase genes celF and celD.
Transcripts of the Clostridium thermocellum endoglucanase genes celF and celD, encoding endoglucanases F and D, respectively, were characterized. The size of the mRNAs was about 2.35 kb for celF and 2.1 kb for celD, indicating monocistronic transcription of both genes. A unique 5' end, located 218 bp upstream from the initiation codon, was found for celF mRNA. No convincing homology could be id...
متن کاملCharacterization of endoglucanase A from Clostridium cellulolyticum.
A construction was carried out to obtain a high level of expression in Escherichia coli of the gene celCCA, coding for the endoglucanase A from Clostridium cellulolyticum (EGCCA). The enzyme was purified in two forms with different molecular weights, 51,000 and 44,000. The smaller protein was probably the result of proteolysis, although great care was taken to prevent this process from occurrin...
متن کاملPurification and specificity of cellobiose phosphorylase from Clostridium thermocellum.
A nonspecific cellobiose phosphorylase from Clostridium thermocellum, which has been purified over loo-fold, is active on 10 different glucosyl acceptors, D-glucose, Z-deoxyglucose, 6-deoxyglucose, D-glucosamine, D-mannose, D-a&rose, L-galactose, L-fucose, D-arabinose, and D-xylose. Following electrophoresis on polyacrylamide gels, the activity with various acceptors occurs at the location of t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1991
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2790067