Degradative acetolactate synthase of Bacillus subtilis: purification and properties
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منابع مشابه
Purification and properties of fructose-1,6-bisphosphatase of Bacillus subtilis.
Fructose-1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrase, EC 3.1.3.11) of Bacillus subtilis is a constitutive enzyme that was purified 1000-fold (30% yield) to 80% purity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis where it exhibits a band corresponding to 72,000 daltons. It sediments at 15 S in sucrose density gradients indicating a molecular weight ...
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Bacillus subfilis nucleoside diphosphokinase was purified l,lOO-fold to apparent homogeneity (a single band upon disc gel electrophoresis). Gel filtration through Sephadex G-ZOO indicated an approximate molecular weight of 100,000. The corrected Michaelis constants for the various nucleoside triphosphate substrates ranged from 0.10 fll~ for GTP to 0.42 mM for CTP. Deoxyribonucleoside triphospha...
متن کاملMetabolic flux analysis of Escherichia coli expressing the Bacillus subtilis acetolactate synthase in batch and continuous cultures.
Metabolically engineered Escherichia coli expressing the B. subtilis acetolactate synthase has shown to be capable of reducing acetate accumulation. This reduction subsequently led to a significant enhancement in recombinant protein production. The main focus of this study is to systematically examine the effect of ALS in the metabolic patterns of E. coli in batch and continuous culture. The sp...
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The goal of this research was to isolate and identify the thermostable alkaline protease producing bacteria among several native Iranian microorganisms. At the end of screening program, a Bacillus subtilis BP-36 strain producing thermophilic alkaline protease was isolated from a hot spring in Ardebil province. The target enzyme was purified using a one-step Aqueous two-phase systems (ATPS) prot...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1975
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.121.3.917-922.1975