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Bacillus subtilis strain

Figure 11.3 Positive ion FIESMS spectra of crude cell extracts from Escherichia coli HB101 (A), Bacillus sphaericus DSM 28 (B), and Bacillus licheniformis NTCC 10341 (C). (D) A pseudo-3D plot of the first three discriminant functions (DF1-3) obtained from positive ion whole-cell DIESMS spectra of seven Bacillus subtilis strains (a-g) (E) the corresponding abridged dendrogram obtained from the same information as in D. (Adopted from Vaidyanathan et al.57)... Figure 11.3 Positive ion FIESMS spectra of crude cell extracts from Escherichia coli HB101 (A), Bacillus sphaericus DSM 28 (B), and Bacillus licheniformis NTCC 10341 (C). (D) A pseudo-3D plot of the first three discriminant functions (DF1-3) obtained from positive ion whole-cell DIESMS spectra of seven Bacillus subtilis strains (a-g) (E) the corresponding abridged dendrogram obtained from the same information as in D. (Adopted from Vaidyanathan et al.57)...
Leenders, F. Stein, T. H. Kablitz, B. Franke, P Vater, J. Rapid typing of Bacillus subtilis strains by their secondary metabolites using matrix-assisted laser desorp-tion/ionization mass spectrometry of intact cells. Rapid Comm. Mass Spectrom. 1999,13, 943-949. [Pg.272]

An extracellular RNase of Bacillus subtilis strain H was isolated in crystalline state and its chemical nature studied by Nishimura and coworkers (112). It has a very complicated base specificity (113, 114)-However, with a few exceptions, the phosphodiester bonds of 3 -purine nucleotides are cleaved faster than those of 3 -pyrimidine nucleotides, and those of 3 -nucleotides with 6(4)-keto group are cleaved faster than those of 3 -nucleotides with a 6(4)-amino group. Thus, when adjacent bonds are the same, the following results ... [Pg.239]

Nishimura and Maruo (118) extracted and RNase from cells of Bacillus subtilis strain H, which is quite different from the extracellular RNases of the same strain. It is remarkable that the digestion products of RNA by the enzyme are exclusively four nucleoside 2, 3 -cyclic phosphates. [Pg.240]

Among the microbial surfactant producers, Bacillus subtilis strains generate a lipopeptide called surfactin, one of the most effective biosurfactants known. This biomolecule is usually a cyclic compound consisting of seven amino acids bonded to a lipid moiety. Surfactin is effective in lowering the surface tension of water to <30 dyn/cm (17), which is comparable with the values obtained by conventional synthetic surfactants. Additionally, surfactin preparations have other interesting characteristics, including antibiotic and antiviral properties (18). In fact, surfactin is one of the few biosurfactants that has found commercial use (19). [Pg.900]

For growth of competent recipient Bacillus subtilis strain 168 (Trp-) ... [Pg.340]

Inoculate 5 ml of 0.8% nutrient broth, 0.5% glucose, and 50 /Ug/ml tryptophan with a sample of Bacillus subtilis strain 168 (Trp-) obtained from a stock culture slant. [Pg.340]

Trace Metal Uptake by Bacillus subtilis Strain 168... [Pg.172]

Widner, W. Behr, R. Sloma, A. DeAngelis, P. L. Weigel, P. Guillaumie, F. Brown, S. Hyaluronic acid production by recombinant Bacillus subtilis strains ACS Polymer Preprints, 2006, 47(2), 213. [Pg.16]

Pohl, S. et al (2013) Proteomic analysis of Bacillus subtilis strains engineered for improved production of heterologous proteins. Proteomics, 13 (22), 3298-3308. [Pg.285]

Manabe, K. etal. (2011) Combined effect of improved cell yield and increased specific productivity enhances recombinant enzyme production in genome-reduced Bacillus subtilis strain MGB874. Appl. Environ. Microbiol, 77 (23), 8370-8381. [Pg.290]

Qian, J. et al (2006) Nucleotide mutations in purA gene and pur operon promoter discovered in guanosine-and inosine-producing Bacillus subtilis strains. Biotechnol Lett., 28 (12), 937-941. [Pg.294]

The physical appearance and microscopic examination revealed that the films deteriorated in soil. Blends in the Bacillus subtilis strain showed more degradation as compared to the Escherichia Coli strain (25). [Pg.53]

Kubo, Y, Rooney, A. P, Tsukakoshi, Y, Nakagawa, R., Hasegawa, H., Kimura, K. (2011). Phylogenetic analysis of Bacillus subtilis strains applicable to Natto (fermented soybean) production. Applied and Environmental Microbiology, 77, 6463-6469. [Pg.173]

RawatR, TewariL. (2012). Purification and characterization of an acidothermophihc ceUulase enzyme produced by Bacillus subtilis strain LFS3. Extremophiles, 16, 637-644. [Pg.130]

Yeh CM, Wang JP, Lo SC, Chan WC, Lin MY. (2010). Chromosomal integration of a synthetic expression control sequence achieves poly-y-glutamate production in a Bacillus subtilis strain. Biotechnol Prog, 26, 1001-1007. [Pg.496]

Yao D, Ji Z.Wang C, Qi G, Zhang L, Ma X, et al. Co-producing iturin A and poly-y-glutamic acid from rapeseed meal under solid state fermentation by the newly isolated Bacillus subtilis strain 3-10. World J Microbiol Biotechnol 2012 1—7. [Pg.388]

Fig. 7.7 Dendrograms calculated on the basis of cluster analysis of MALDI-TOF mass spectra of 28 Bacillus subtilis strains of two ecotypes (PE 10 and PE32) using a standard sample preparation protocol and b microwave-assisted digestion... Fig. 7.7 Dendrograms calculated on the basis of cluster analysis of MALDI-TOF mass spectra of 28 Bacillus subtilis strains of two ecotypes (PE 10 and PE32) using a standard sample preparation protocol and b microwave-assisted digestion...
Biodegradation of blends of pofy(e-caprolaetone) (PCL) with poly(vit5 l butyral) (PVB) blends was studied in the soil and by baeterial strains of Bacillus subtilis and Escherichia coli isolated from the soil [135]. Weight loss was observed in all the blends. PCL-rich blends showed more degradation, which was faster in the natural environment than in the laboratory. Blends in the Bacillus subtilis strain showed more degradation as eompared to the E. coli strain. [Pg.155]

Yamazaki, H., Ohmura, K., Nakayama, A., Takeichi, Y., Otozai, K., Yamasaki, M., Tamura, G. and Yamane, K., 1983, Amylase genes (amyR2 and amyE) from an a-amylase-hyperproducing Bacillus subtilis strain molecular cloning and nucleotide sequences, J. Bacterlol., 156 327. [Pg.13]


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See also in sourсe #XX -- [ Pg.34 ]




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