Improved Production of Mannanase by Streptomyces lividans
نویسندگان
چکیده
منابع مشابه
Recombinant production of Streptococcus equisimilis streptokinase by Streptomyces lividans
BACKGROUND Streptokinase (SK) is a potent plasminogen activator with widespread clinical use as a thrombolytic agent. It is naturally secreted by several strains of beta-haemolytic streptococci. The low yields obtained in SK production, lack of developed gene transfer methodology and the pathogenesis of its natural host have been the principal reasons to search for a recombinant source for this...
متن کاملEngineering of primary carbon metabolism for improved antibiotic production in Streptomyces lividans.
Deletions were made in Streptomyces lividans in either of two genes (zwf1 and zwf2) encoding isozymes of glucose-6-phosphate dehydrogenase, the first enzyme in the oxidative pentose phosphate pathway (PPP). Each mutation reduced the level of Zwf activity to approximately one-half that observed in the wild-type strain. When the mutants were transformed with multicopy plasmids carrying the pathwa...
متن کاملMetabolomics investigation of recombinant mTNFα production in Streptomyces lividans
BACKGROUND Whilst undergoing differentiation, Streptomyces produce a large quantity of hydrolytic enzymes and secondary metabolites, and it is this very ability that has focussed increasing interest on the use of these bacteria as hosts for the production of various heterologous proteins. However, within this genus, the exploration and understanding of the metabolic burden associated with such ...
متن کاملSingle Streptomyces lividans K+ Channels
Basic electrophysiological properties of the KcsA K(+) channel were examined in planar lipid bilayer membranes. The channel displays open-state rectification and weakly voltage-dependent gating. Tetraethylammonium blocking affinity depends on the side of the bilayer to which the blocker is added. Addition of Na(+) to the trans chamber causes block of open-channel current, while addition to the ...
متن کاملLarge-scale production of a thermostable Rhodothermus marinus cellulase by heterologous secretion from Streptomyces lividans
BACKGROUND The gene encoding a thermostable cellulase of family 12 was previously isolated from a Rhodothermus marinus through functional screening. CelA is a protein of 260 aminoacyl residues with a 28-residue amino-terminal signal peptide. Mature CelA was poorly synthesized in some Escherichia coli strains and not at all in others. Here we present an alternative approach for its heterologous ...
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: Applied and Environmental Microbiology
سال: 1996
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.62.12.4656-4658.1996