• Journal of Microbiology and Biotechnology
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• v.14 no.4
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• pp.751-758
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• 2004

The NCS(Non-Cariogenicity Sugar) from Bacillus sp. S-1013 was purified by cold acetone and methanol precipitation, and DEAE-cellulose ion-exchange and Sephadex G-100 column chromatographies, to yield an amorphous yellow syrup. The melting point and $[\alpha]_D^{20}$ were 155-$157^{\circ}C$ and +53, respectively. Instrumental analyses such as FT-IR, $^1H-NMR, and ^{13}C-NMR$ showed that the NCS contained an O-H group, C-H, C=O, $NH_2$, anomeric carbon, anomeric proton, N-acetylgalactose, fucose, and neuramic acid, thus, the NCS was determined to be a trisaccharide of Fuc($1\longrightarrow4$)GalNAc($2\longrightarrow6$) NeuAc.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2000.06a
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• pp.92-92
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• 2000

• Journal of Microbiology and Biotechnology
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• v.11 no.4
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• pp.712-715
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• 2001

A new combined method including the enzymatic hydrolysis of $\beta$-cyclodextrin ($\beta$-CD) and solvent extraction fo cholesterol from the hydrolyzed mixture was developed to recover cholesterol from a $\beta$-CD-cholesterol complex prepared from dairy products, such as cream, milk, and cheese. Cyclomaltodextrinase (cyclomatodextrin dextrin hydrolase, EC 3.2.1.54, DCase_ prepared form alkalophilic Bacillus sp. KJ 133 hydrolyzed the $\beta$-DC of the $\beta$-CD-cholesterol complex, and then, free cholesterol was efficiently extracted from the hydrolyzed mixture by a nonpolar solvent such as ethyl acetate. To increase the stability of free CDase, immobilized CDase was developed using sodium alginate as a carrier. The immobilized CDase showed a high recovery yield of cholesterol in a time-dependent manner compared to the free CDase. A gas chromatography analysis showed that more than 70% of cholesterol was recovered from the $\beta$-DC-cholesterol complex of cream by the immobilized CDase, whereas only 3% and 29% of cholesterol were recovered when the solvent extraction and free CDase treatment were used, respectively. The cholesterol recovered can be used as a raw material for steroid synthesis. Furthermore, this method can be an efficient way to recover cholesterol or other organic compounds that are bound in a $\beta$ -DC-cholesterol or -organic compound complex.

• 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.

• Korean Journal of Food Science and Technology
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• v.23 no.3
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• pp.349-354
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• 1991

An alkaline amylase-producing Bacillus sp. GM8901 was isolated and some properties of crude enzyme extract were examined. The microbiological and biochemical characteristics of GM8901 were very similar to those of B. licheniformis. The optimal temperature and pH for the cell growth and amylase production were $50^{\circ}C$ and pH 10.5. The crude amylase extract showed that the optimal temperature and pH were $50{\sim}60^{\circ}C\;and\;pH\;10{\sim}12$, respectively, and that the activity of amylase was stable up to $50^{\circ}C$ and in the range of $pH\;3{\sim}12$.

• Microbiology and Biotechnology Letters
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• v.18 no.4
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• pp.344-351
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• 1990

An alkalophilic microoganism producing a detergent-resistant alkaline protease was isolated from soil and identified as Baeiltus sp. The alkaline protease has been partially purified by ammonium sulfate fractionation, DEAE-Cellulose, CM-Cellulose and Sephdex G-100 column chromatography. The purified alkaline protease was highly active at pH 12-13 toward casein and stable at pH values from 6 to ll. The optimum temperature for the enzyme reaction was $55^{\circ}C$. The enzyme was completely inactivated by diisopropyl fluorophosphate (DFP) indicating that the enzyme was serine protease, but considerabiy stable in the presence of surface active agents.

• Journal of Microbiology and Biotechnology
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• v.5 no.4
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• pp.206-212
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• 1995

A strain BL-29, which produces a extracellular lytic enzyme on E. coli was isolated from the soil. The strain was identified as belonging to the genus Bacillus sp. The lytic enzyme was purified to homogeneity by ion exchange chromatography and gel filtration. Specific activity of the purified enzyme was 28, 850 U/mg protein and yield of the enzyme was 5$%$. The purified enzyme showed a single band on SDS-PAGE and its molecular weight was estimated to be 31, 000 by SDS-polyacrylamide gel electrophoresis and gel filtration column chromatography. The optimum temperature and pH were $55^{\circ}C$ and pH 10.0, respectively. The enzyme was stable at $45^{\circ}C$ but enzyme activity was reduced by up to 50$%$ when the temperature was raised to $55^{\circ}C$ for 15 min. Stable range of pH was from 5.0 to 11.0. but Enzyme activity was inhibited by lead-acetate, mercuric chloride, ethylene glycol-bis-[$\beta$-aminoethyl ether]-N, N, $N^1, $N^1$-tetraacetic acid (EGTA), and ethylenediamine tetraacetic acid (EDTA), but not affected considerably by treatment with other chemical reagents.

• Journal of Microbiology and Biotechnology
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• v.14 no.4
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• pp.759-765
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• 2004

The NCS inhibited the activity of glucosyltransferase which was produced by Streptococcus mutans JC-2, and the rate of inhibition at $100\muM<$ and $200\muM$ were 74.0% and 99.8%, respectively. It was stable in alkali condition, but unstable in acid condition. It was also stable up to $80^{\circ}C$. The kinetic study of the inhibition by NCS was carried out by Lineweaver-Burk plot and Dixon plot. It was non-competitive inhibition, determined by the two plots and $K_i$ and $K_i$ values were $15\muM$ and $19.3\muM$ respectively. The NCS did not show cytotoxicity against human gingival cells at $K_i$ ($15\muM$, $150\muM$, $1,500\mu$ M) concentrations. It had less cytotoxicity than chlohexidin, which has usually been used as the agent of anticaries. To evaluate the industrial applicability of the NCS, human pluck tooth was used. The inhibitory rates of tooth calcification and calcium ion elution by the NCS were 41 % and 2.5 times, respectively. These results suggested that NCS from Bacillus sp. S-1013 is an efficient anticaries agent.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.532.2-532
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• 1986

Alkaline protease which is an important enzyme used in detergents, leather tanning and food industry was produced by alkalophilic bacterium, Bacillus sp. KCTC 1723 isolated from soil. The maximum productivity of the enzyme in alkaline medium containing 1% sodium bicarbonate was obtained by incubating for 3 days at 37$^{\circ}C$. The optimum pH of the enzyme was 11.5 and calcium ion was effective on stabilization of the enzyme at high temperature. The enzyme was not inhibited by metal chelating agent such as El)TA but inhibited by diisopropyl fluorophosphate. Purification of the enzyme was carried out DEAE- and CM-cellulose column chromatographies and molecular weight of the purified enzyme was determined

• Microbiology and Biotechnology Letters
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• v.23 no.6
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• pp.687-694
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• 1995

Alkalophilic Bacillus sp. HJ-12 producing $\beta $-1, 4-D-arabinogalactanase was isolated from soil in the alkalic condition, pH 10.0. $\beta $-1, 4-D-arabinogalactanase was maximaly produced in the medium consisting of 2% soybean arabinogalactan (SAG), 0.5% yeast extract, 0.5% polypeptone, 0.5% NaCl, 0.1% K$_{2}$HPO$_{4}$, 0.02% MgSO$_{4}$$\cdot $7H$_{2}$O, 0.1% Na$_{2}$CO$_{3}$ under the aerobic condition (pH 8.2). $\beta $-1, 4-D-arabinogalactanase is inducible enzyme so that its activity has been increased 10 fold in the SAG medium than in the glucose medium. Through the ammonium sulfate precipitation, DEAE- Sephadex A-50 ion chromatography, and Sephadex G-75 gel chromatography procedures, this enzyme was purified with a single protein of 11% vield and 110 fold's purity. $\beta $-1, 4-D-arabinogalactanase is endo type enzyme producing ollgosaccharide from SAG.