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Thermophiles genes

Kucho, K.-I., Y. Tsuchiya, Y. Okumoto et al. (2004). Construction of unmodified oligonucleotide-based arrays in the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 Screening of the candidates for circadianly expressed genes. Genes Genet Syst 79 319-329. [Pg.16]

Kirimura, K. Harada, K. Iwasawa, H., et al., Identification and Functional Analysis of the Genes Encoding Dibenzothiophene-Desulfurizing Enzymes From Thermophilic Bacteria. Applied Microbiology and Biotechnology, 2004. 65(6) pp. 703-713. [Pg.208]

Ohshiro, T. Yamada, H. Shimoda, T., et al., Thermostable Flavin Reductase That Couples With Dibenzothiophene Monooxygenase, From Thermophilic Bacillus Sp DSM411 Purification, Characterization, and Gene Cloning. Bioscience Biotechnology and Biochemistry, 2004. 68(8) pp. 1712-1721. [Pg.213]

Ishii, Y. Konishi, 1 Suzuki, M., and Maruhashi, K., Cloning and Expression of the Gene Encoding the Thermophilic NAD(P)H-FMN Oxidoreductase Coupling With the Desulfurization Enzymes From Paenibacillus Sp All-2. Journal of Bio science and Bioengineering, 2000. 90(6) pp. 591-599. [Pg.213]

Figure 14.3. Composition and structural organization of atp genes in E. coli (Ecoli) (accession no. J01594), thermophilic bacterium PS3 (PS3) (accession no. X07804), C. pasteurianum (Cpast) (accession no. AF283808), M. thermoacetica (Mthe) (accession no. U64318), and A. woodii. (Awoo) (U10505). The size of each gene (in base pairs) is also shown. Figure 14.3. Composition and structural organization of atp genes in E. coli (Ecoli) (accession no. J01594), thermophilic bacterium PS3 (PS3) (accession no. X07804), C. pasteurianum (Cpast) (accession no. AF283808), M. thermoacetica (Mthe) (accession no. U64318), and A. woodii. (Awoo) (U10505). The size of each gene (in base pairs) is also shown.
Special attention has been paid by sevo groups to cloning xylanase genes from thermophilic microorganisms as a source of thermostable xylanases. Cloning of such genes in mesophilic recepients offers a convenient way to purify xylanases simply by a heat denaturation of the more heat-labile proteins of the host (54). Applications are limited to those enzymes that possess thermostability considerably higher than the majority of the host cell proteins. [Pg.412]

Yaklichkin, S.Y. Zimina, M.S. Neumyvakin, L.V, Proline biosynthesis gene proB of thermophilic bacterium Thermus ruber cloning, sequencing, and properties of encoded y-glutamylphosphate kinase. Mol. Biol., 33, 628-635 (1999)... [Pg.357]

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Thermophiles

Thermophilic

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