• 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.

• Microbiology and Biotechnology Letters
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• v.23 no.2
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• pp.197-202
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• 1995

The conditions for the $\beta$-fructofuranosidase production from alkalophilic, thermophilic Bacillus sp. TA-11 were investigated. The maximal enzyme production was obtained when the strain was cultured at 50$\circ$C for 36 hrs with batch culture in the optimal medium containing 1.0% sucrose, 0.6% yeast extract, 0.1% each of KH$_{2}$PO$_{4}$, K$_{2}$HP0$_{4}$, NaH$_{2}$PO$_{4}$, and initial pH 9.5, and the final enzyme activity under the above condition was 102 units per ml of cell free extract.

• 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.9 no.4
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• pp.447-451
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• 1996

Lytic activities of the egg white lysozyme from Korea-native Ogol fowl against the alkalophilic and thermophilic Bacillus sp. TA-11 were investigated and compared. Lytic activity of the Ogol fowl lysozyme for Bacillus sp. TA-11 was the highest for the cell of post-logarithm phase and optimum concentration of the lysozyme was 0.25%, Optimum reaction pH and temperature were 4.5 and 35$^{\circ}C$, respectively. Lytic activity of egg white lysozyme from fowl for Bacillus sp. TA-11 was the highest for the cell of stationary phase and optimum concentration of the lysozyme was 0.5%. Optimum reaction pH and temperature were 5.5 and 4$0^{\circ}C$, respectively.

• Microbiology and Biotechnology Letters
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• v.34 no.4
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• pp.318-322
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• 2006

The intracellular invertase gene of alkalophilic and thermophilic Bacillus sp. TA-11 which was isolated from compost was cloned and expressed in E. coil HB101 using pUC19 as a vector. The invertase of the recombinant E. coli (pYC 17) was maximally produced when it was incubated at 37$^{\circ}C$ for 9 h in a SY medium containing 0.25% sucrose, 0.5% yeast extract, 0.1% each of $K_2HPO_4$ and $KH_2PO_4$, with an initial pH of 8.0. The final enzyme activity under the above condition was 47.7 U per ml of cell-free extract.

• The Journal of Natural Sciences
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• v.5 no.2
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• pp.13-17
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• 1992

Regulation of $\beta$-galactosidase biosynthesis was studied with alkalophilic, thermophilic Bacillus sp. TA-11. Biosynthesis of the enzyme was effectively induced by lactose and some low level by isoprophyl-$\beta$-D-thiogalactopyranoside(IPTG). When 30mM glucose was added at the different intervals to the culture that had been in contact with lactose, the different levels of the enzyme synthesis were observed. So, this suggests that glucose interfered with the entry of the lactose into the cells.The glucose inhibitory effect was not relieved by adding cAMP to the culture.

• KSBB Journal
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• v.9 no.4
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• pp.400-405
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• 1994

The conditions for ${\beta}$-galactosidase production from alkalophilic, thermophilic Bacillus sp. TA-11 were investigated. The maximal enzyme production was obtained when the strain was cultured at $50^{\circ}C$ for 5 days with fed-batch culture in the optimal medium containing 1.5% lactose, 0.6% yeast extract 0.15% $K_2HP0_4$and initial pH 9.5, and then final enzyme activity under the above conditions was 5200 unit/ml of cell free extract.

• 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).