• Journal of Microbiology and Biotechnology
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• v.3 no.4
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• pp.224-231
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• 1993

The nucleotide sequence of the xylanase gene (xynY) from alkalophilic Bacillus sp. YC-335 was determined and analyzed. An open reading frame of 1, 062 base pairs for xynY gene was observed and encoded for a protein of 354 amino acids with a molecular weight of 38, 915. S1 nuclease mapping showed that the transcription initiation sites of the xynY gene were different in Bacillus sp. YC-335 and Escherichia coli HB101 (pYS55). S1 mapping also showed that -10 region of the xynY gene recognized by RNA polymerases of E. coli and Bacillus sp. YC-335 were TACAGT and TATGAT , respectively. A ribosome binding site sequence with the free energy of -17.0 Kcal/mol was observed 9 base pairs upstream from the unusual initiation codon, TTG. The proposed signal sequence consisted of 27 amino acids, 2 of which were basic amino acid residues and 21 were hydrophobic amino acid residues. When the amino acid sequences of xylanases were compared, Bacillus sp. YC-335 xylanase showed more than 50% homology with xylanases from B. pumilus, B. subtilis, and B. circulans.

• Journal of Applied Biological Chemistry
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• v.50 no.4
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• pp.196-201
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• 2007

An intracellular invertase was purified to homogeneity from the cell extract of an alkalophilic and thermophilic Bacillus sp. TA-11, which was classified as a new species belonging to Bacillus cereus based on chemotaxanomic and phylogenetic analyses. The purified enzyme with a recovery of 26.6% was determined to be a monomeric protein with a molecular weight of 23 kDa by SDS-PAGE and 26 kDa by gel filtration. The maximum enzyme activity was observed at pH 7.0 and $50^{\circ}C$, and the purified enzyme was stable at the pH range of 5.0 to 8.0 and below $60^{\circ}C$. $K_m$ and $V_{max}$ values of the enzyme for sucrose were 370 mM and 3.0 ${\mu}M$ per min, respectively. The enzyme activity was significantly inhibited by bivalent metal ions ($Hg^{2+}$, $Cd^{2+}$ and $Cu^{2+}$) and sugars (glucose and fructose).

• The Journal of Natural Sciences
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• v.5 no.1
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• pp.47-52
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• 1992

A alkalophilic, thermophilic bacterium TA-11 which produce $\beta$-galactosidase highly was isolated from compost and identified to the genus Bacillus. $\beta$-galactosidase production was maximized when it was incubated in synthetic medium containing 1.5% lactose. 0.4% peptone, 0.4% teast ext., 0.2% $MgSO_4$ 0.05% $NH_4$Cl and 0.2% NacL(initial pH; 10.0) at $50^{\circ}C$ for 2 days in reciprocal shaker.

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.99-99
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• 1995

No Abstract, See Full Text

• Journal of Microbiology and Biotechnology
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• v.3 no.2
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• pp.73-77
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• 1993

The nucleotide sequence of Bacillus sp. bacteriolytic enzyme gene, lytP and its flanking regions were determined. A unique open reading frame for a protein of Mw. 27, 000, and a putative terminator sequence, were found behind a concensus ribosome binding site located 8 nt upstream from ATG start codon. The primary amino acid sequence deduced from nucleotide sequence revealed a putative protein of 255 amino acid residues with an Mw. of 27, 420. No significant homology could be found between the amino acid sequence of Bacillus sp. bacteriolytic enzyme and that of other cell wall hydrolases.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.529.1-529
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• 1986

For isolation of the CMCase gene of the alkalophilic Bacillus sp. strain N-4 to analyze their genetic information for the multicomponents of the cellulase, Bscherichia coli K12 and plasmid DNA pBR322 was used as host-vector system. After the digestion of purified chromosomal DNA and plasmid DNA pBR322 with HindIII, these were ligated. The ligated DND were transformed into Escherichia coli, and recombinant plasmid 107 carried the gene coding for CMCase was constructed. The CMCase produced by Escherichia coli cells containing plasmid DNA pYBC107 was found in the cells as intracellular enzyme and nearly 60% of the total CMCase activity was localized in cellular fraction. Also, the optimum pH for the reaction of CMCase produced by Escherichia coli was appeared at pH .8.0 and the enzyme was stable between pH 7.0 and pH 8.0.

• Journal of Industrial Technology
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• v.7
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• pp.59-68
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• 1987

In order to obtain a strain of producing lipase which has resistance against alkaline and detergent, a screening test was carried out. Among 500 strains isolated from soil samples, the strain J-19 was selected for this study. The composition of the optimum medium for the highest lipase production was 2.0% glycerin, 1.0% corn steep liquor, 2.0% yeast extract, 0.1% $MgSO_4$ $7H_2O$, 0.2% $K_2HPO_4$, 1.5% soybean oil and 0.1% LAS(linear alkylbenzene sulfonate) with initial pH value of 10.0 and 3-day cultivation at $25^{\circ}C$. The lipase activity of the strain J-19 under optimal condition was 3.3. units/ml, which was increased about 1.3-fold than that of basal medium.

• The Korean Journal of Food And Nutrition
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• v.15 no.2
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• pp.126-130
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• 2002

Regulation of invertase biosynthesis was studied in thermophilic and alkalophilic Bacillus sp. TA-11. Biosynthesis of the invertase was effectively induced in the presence of 10 mM sucrose for 180 min. Glucose repressed the invertase induction by sucrose and as late as addition time of glucose, the invertase formation was increased, indicating that glucose repression was occurred by inducer exclusion. Catabolite repression was reduced a little by the addition of cAMP for 180 min of induction.

• The Korean Journal of Food And Nutrition
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• v.2 no.1
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• pp.1-11
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• 1989

Glucose isomerase (E.C.5.3.1.5) which reversibly catalyzes reaction between D-glucose and D-fructose was demonstrated in cell free extracts of alkalophilic Streptomyces sp. B-2 isolated from soil The optimum temperature, pH, and pH stability were 6$0^{\circ}C$, 10.5, and 7.8, respectively. The production of Gl in xylose and yeast extract was higher than that of other carbon source and nitrogen source. The Gl production was affected by Co2+ and Mg2).

• The Korean Journal of Food And Nutrition
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• v.1 no.2
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• pp.68-75
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• 1988

A strain of alkalophilic Bacillus sp. YS-309 has been isolated from domestic soil. It belongs to genus Bacillus from its morphological and biochemical characteristics. The strain grows better in the alkaline media rather than in the neutral media. The optimum pH and temperature for growth were observed at 8.5 and 4$0^{\circ}C$, respectively. Glucose, lactose and maltose were appeared as good carbon source but soluble starch and fructose were utilized uneffectively for growth. Concentrations of lactose had affected both the cellular growth and the enzyme productions. The maximum growth and the highest enzyme productions were obtained at 0.5%(w/e) of lactose added in the media. B-Galactosidase from Bacillus sp. YS-309 was produced inducibly into the cell and total enzyme activities per ml were gradually decreased when the concentration of glucose increased.