Bacillus megaterium--from simple soil bacterium to industrial protein production host.
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Authors
Vary, Patricia SBiedendieck, Rebekka
Fuerch, Tobias
Meinhardt, Friedhelm
Rohde, Manfred
Deckwer, Wolf-Dieter
Jahn, Dieter
Issue Date
2007-10
Metadata
Show full item recordAbstract
Bacillus megaterium has been industrially employed for more than 50 years, as it possesses some very useful and unusual enzymes and a high capacity for the production of exoenzymes. It is also a desirable cloning host for the production of intact proteins, as it does not possess external alkaline proteases and can stably maintain a variety of plasmid vectors. Genetic tools for this species include transducing phages and several hundred mutants covering the processes of biosynthesis, catabolism, division, sporulation, germination, antibiotic resistance, and recombination. The seven plasmids of B. megaterium strain QM B1551 contain several unusual metabolic genes that may be useful in bioremediation. Recently, several recombinant shuttle vectors carrying different strong inducible promoters and various combinations of affinity tags for simple protein purification have been constructed. Leader sequences-mediated export of affinity-tagged proteins into the growth medium was made possible. These plasmids are commercially available. For a broader application of B. megaterium in industry, sporulation and protease-deficient as well as UV-sensitive mutants were constructed. The genome sequence of two different strains, plasmidless DSM319 and QM B1551 carrying seven natural plasmids, is now available. These sequences allow for a systems biotechnology optimization of the production host B. megaterium. Altogether, a "toolbox" of hundreds of genetically characterized strains, genetic methods, vectors, hosts, and genomic sequences make B. megaterium an ideal organism for industrial, environmental, and experimental applications.Citation
Bacillus megaterium--from simple soil bacterium to industrial protein production host. 2007, 76 (5):957-67 Appl. Microbiol. Biotechnol.Affiliation
Department of Biological Sciences, Northern Illinois University, DeKalb, IL 60115, USA.PubMed ID
17657486Type
ArticleLanguage
enISSN
0175-7598ae974a485f413a2113503eed53cd6c53
10.1007/s00253-007-1089-3
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