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Bacillus subtilis intracellular

Mycobacteria are more resistant than other non-sporulating bacteria to a wide range of biocides. Examples of such organisms axe Mycobacterium tuberculosis, theM avium-intracellulare (MAI) group andM. chelonae (M. chelonei). Of the bacteria, however, the most resistant of all to biocides are bacterial spores, e.g. Bacillus subtilis, B. cereus. [Pg.264]

The ATP test is a bioluminescence procedure based on the reaction between adenosine-5-triphosphate (ATP) and a luciferin-luciferase enzymatic system (42, 43). The principle of the test relies on the fact that after a certain incubation period the intracellular ATP level, which gives a reliable indication of the state of development of a suitable bacterial culture (44), will remain low relative to a control, when antimicrobial residues are present. In its first version the ATP test employed Bacillus subtilis ATCC 6633 as the test organism, but a current version is based on the use of Streptococcus thermophilus T.J. culture. [Pg.803]

The host bacteria used for production of recombinant proteins are usually E. coli, or Bacillus subtilis they may express proteins at 1 % to over 50% of the cellular protein, depending on such variables as the source, promoter structure, and vector type. Generally the proteins are expressed intracellularly, but leader sequences for excretion may be included. In the latter case, the protein is generally excreted into the periplasmic space, which limits the amount that can be produced. Excretion from grampositive species such as B. subtilis sends the product into the culture medium, with little feedback limitation on total expression level. [Pg.277]

The same enzyme has been highly purified from another strain (strain K) of Bacillus subtilis, and their properties have been fully investigated by Yamasaki and Arima (119, 120). They have confirmed the findings by Nishimura and Maruo and have found, moreover, that ATP and dATP strongly inhibit the enzyme. Yamasaki and Arima suggested that ATP might participate in the regulation of intracellular RNase activity. [Pg.240]

Methodological approaches to help unravel the intracellular metabolome of Bacillus subtilis. Microb. Cell Fact., 12 (1), 69. [Pg.215]

Spihmbergo, S. Bertucco, A. Basso, G. Bertoloni, G. Determination of extracellular and intracellular pH of Bacillus subtilis suspension under CO2 treatment. Biotechnol. Bioeng. 2005,92,447-451. [Pg.119]

McAllister, W. T., Green, D. M. Bacteriophage SP82G inhibition of an intracellular deoxyribonucleic acid inactivation process in Bacillus subtilis. J. Virol. 10, 51-59... [Pg.86]


See other pages where Bacillus subtilis intracellular is mentioned: [Pg.296]    [Pg.427]    [Pg.112]    [Pg.41]    [Pg.265]    [Pg.232]    [Pg.329]    [Pg.422]    [Pg.61]    [Pg.280]    [Pg.415]    [Pg.548]    [Pg.381]    [Pg.75]    [Pg.93]    [Pg.217]    [Pg.127]    [Pg.78]    [Pg.378]    [Pg.149]    [Pg.291]    [Pg.15]    [Pg.248]    [Pg.316]    [Pg.657]    [Pg.128]    [Pg.251]    [Pg.257]   
See also in sourсe #XX -- [ Pg.240 ]




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Bacillus subtilis

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