• Microbiology and Biotechnology Letters
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• v.25 no.5
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• pp.477-482
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• 1997

To investigate the cytotoxicity of Korean traditional fermented soybean products using the MTT assay, we extracted soybean, Kanjang, Doenjang, Kochujang, and Chongkukjang with water, methanol, and hexane. Primary testing of cytotoxicity of 14 extracts was done for P388D1(mouse lympoid neoplasm) and L1210(mouse leukemia) cell lines. Doenjang methanol extract, Kochujang hexane extract, Chongkukjang methanol extract, and Chongkukjang hexane extract showed cytotoxicity of 86.1, 94.3, 83. 6, and 81.1%, respectively against P388D1, and showed cytotoxicity of 69.4, 96.9, 51.4, and 95.1%, respectively against L1210. All the other extracts showed less than 50% cytotoxicity. Methanol extracts of Doenjang and Chongkukjang showed dose-dependent cytotoxicity against P388DI, L1210, SNU-16 (human stomach cancer), HepG2(human hepatic cancer), WiDr(human colon cancer) cell lines, and IC$_{50}$ of Doenjang methanol extract was 67.7, 90.4, 1338.0, 706.4, and 371.2 $\mu$g/ml, respectively, and IC$_{50}$ of Chongkukjang methanol extract was 107.1, 228.3, 756.2, 1346.0, and 327.0 $\mu$g/ml, respectively.

• Microbiology and Biotechnology Letters
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• v.22 no.2
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• pp.120-125
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• 1994

By using a synthetic medium simulated on the amino acid composition of soybeam, the effect of salt concentrations on the production of volatile organic acid by the strains of Zygosaccharomyces rouxii So-3101, a soy sauce yeast, was studied at the concentrations of 12.5, 18.0, 22.0 and 28.5% NaCl. The growth, consumption of glucose, and production of alcohol, total acid and volatile organic acid, showed the highest values at a concentration of 12.5% NaCl, and those values were decreased with an increase in the salt concentration. The ratio of volatile organic acid to total organic acid was remained at approximately the same level within the range of salt concentrations between 12.5~22.0%, whereas the ratio was decreased at a salt concentration of 28.5%. After incubation for 16 days, 8 volatile organic acids, i.e. acetic, propionic, n-butyric, isobutyric, isovaleric, isocaproic, n-caproic, and heptanoic acids, were detected by gas chromatography. Among the volatile organic acids, acetic acid was produced in the appreciable amiunt and its ratio to the other volatile acids was increased with an increase in the salt concentration.A small amount of isocaproic, propionic, isobutyric and isovaleric acids were produced, and n-caproic, n-butyric and heptanoic acids were detected only at the lower salt concentration.

• Microbiology and Biotechnology Letters
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• v.30 no.4
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• pp.293-297
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• 2002

The cyclodextrin glucanotransferase (CGTase) gene from Bacillus stearothermophilus NO2 was expressed in Saccharomyces cerevisiae 2805 under the adhl promoter. The CGTase was purified from S. cerevisiae 2805/pVT-CGTS. The purified enzyme exhibited a optima of activity around pH 7.0 and $65^{\circ}C$. Thermal stability of the enzyme was increased fairly as compared with the CGTase of B. stearothermophilus NO2. The conversion yield of cyclodextrin (CD) and the production ratio of $\alpha$-, $\beta$,-, ${\gamma}$-CD from starch were showed similarly aspect to the CGTase of B. stearothermophilus NO2.

• Microbiology and Biotechnology Letters
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• v.23 no.5
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• pp.573-579
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• 1995

A Bacillus strain capable of producing an extracellular malto-oligosaccharides forming $\alpha $-amylase was isolated from soil and designated as Bacillus sp. SUH4-2. The enzyme was purified by ammonium sulfate fractionation, DEAE-Toyopearl and Mono-Q HR 5/5 column chromatographies using a FPLC system. The specific activity of the enzyme was increased by 16.1-fold and the yield was 13.5%. The optimum temperature for the activity of $\alpha $-amylase was 60-65$\circ$C and more than 50% of initial activity was retained after the enzyme was incubated at 60$\circ$C for 40 min. The enzyme was stable over a broad pH range of 5.0-8.0 and the optimum pH was 5.0-6.0. The molecular weight of the enzyme was determined to be about 63.6 kD and isoelectric point was around 5.8. The enzyme activity was strongly inhibited by Mn$^{2+}$, Ni$^{2+}$, and Cu$^{2+}$ ; slightly by Ca$^{2+}$. The purified enzyme produced starch hydrolyzates containing mainly maltose and maltotriose from soluble starch. The starch hydrolyzates were composed of 11% glucose, 59% maltose, 25% maltotriose and 5% maltotetraose.

• Microbiology and Biotechnology Letters
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• v.34 no.4
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• pp.357-362
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• 2006

A growth inhibition assay using Chlorella sp. AG 10002 based on the OECD 201 standard test procedure was applied to the toxicity testing of endosulfan and its reported metabolites. Comparison of dry cell weight, optical density (OD) at 680 nm, and chlorophyll a concentration indicated that optical density at 680 nm of culture broth is convenient, rapid, and accurate method for cell growth. In this microalgae system, the $IC_{50}$ values of endosulfan, endosulfan sulfate, endosulfan lactone, and endosulfan ether were determined as 9.45, 18.8, 18.2 and 37.5 mg/L, respectively. In a while, endosulfan diol did not show a significant toxicity up to 50 mg/L. Since endosulfan is liable at acidic or alkaline conditions, treatment of endosulfan in pH 3, 4, and 11 for 3 days resulted in reduced toxicity, as expected. These results suggested that the microalgae system is useful to evaluate various toxic chemicals and provide a new notion for bioremediation of endosulfan in aqueous systems.

• Microbiology and Biotechnology Letters
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• v.22 no.5
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• pp.515-521
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• 1994

A bacterial strain, which showed the high protease activity at low temperature and the high tolerance for the surfactant, was isolated from soil and identified as Xanthomonas sp. YL-37. The optimal temperature, initial pH, and cultivation time for the production of the alkaline protease by Xanthomonas sp. YL-37 were 20$\circC , 11.0, and 84 hours, respectively. In the jar fermenter culture of Xanthomonas sp. YL-37, the alkaline protease activity was about 15,000 DU/ml/-broth after cultivating for 108 hours. The optimal pH and temperature for the protease activity were 70$\circC and 11.0, respectively. The protease was relatively stable at the pH range of 7.0~12.0 and at the temperatures below 50$\circC . The protease activity at 20$\circC was about the level of 40% of its activity at 70$\circC . The enzyme was suggested as a serine protease because the enzyme activity was inhibited by phenylmethane sulfonyl fluoride, a serine modifier.

• Microbiology and Biotechnology Letters
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• v.22 no.6
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• pp.692-699
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• 1994

A bacterial strain which formed a distinct colony on agar plate containing phenol as a vapor phase and grew well in a liquid minimal medium was isolated and identified as Acinetobac- ter sp. GEM2. The optimal temperature and initial pH for the growth of Acinetobacter sp. GEM2 were 30$\circ$C and 7.0, respectively. Cell growth was inhibited by phenol at the concentration over 1500 ppm. Cell growth dramatically increased from 10 hours after cultivation and almost showed a stationary phase within 24 hours at which 95% of phenol was concomitantly degraded. Acinetobac- ter sp. GEM2 was capable of growing on aromatic compounds, such as benzoic acid, phenol, m- cresol, o-cresol, P-cresol, catechol, gentisic acid, and toluene, but did not grow on benzene, salicylic acid, p-toluic acid, and p-xylene. By the analysis of catechol dioxygenase, it seemed that catechol was degraded through both meta- and ortho-cleavage pathway. The growth-limiting log P value of Acinetobacter sp. GEM2 on organic solvents was 2.0.

• Microbiology and Biotechnology Letters
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• v.27 no.2
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• pp.166-171
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• 1999

This study was conducted to investigate the removal rate of nitrogen and phosphorus, and lipid production from a swine wastewater by Botryococcus braunii UTEX 572 in an outdoor photobioreactor. B. braunii successfully predominated in competition with bacteria and other algae, especially Oscillatoria, which were grown spontaneously in a secondary-treated swine wastewater, under the conditions of incubation temperature at $25^{\circ}C$ and increased inoculum amount at 287mg/l. There was a significant relationship between dry weight of B. braunii and absorbance of culture solution at 680mn(r2=0.967), suggesting that the latter is as good as the former commonly used for the measurement of algal biomass which is considerably time-consuming. The removal rates of COD, TOC, total nitrogen, and total phosphorus from the swine wastewater were 33.2$\pm$2.6% and 32.8$\pm$3.2, respectively, which showing no different between them. These results suggested that the mass cultivation of B. braunii in an outdoor photobioreactor could be used for the advanced treatment of swine wastewater and lipid production.

• Microbiology and Biotechnology Letters
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• v.20 no.2
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• pp.183-189
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• 1992

Cultural conditions of Lactococcus sp. 1112-1, a bacteriocin producing strain, were studied for enhancing its production with regard to environmental and nutritional factors. Optimal compositions of culture medium for bacteriocin production were glucose 20 g/l as carbon source, casein acid hydrolyzate 15 g/l as nitrogen source, and sodium acetate 3 g/l, ammonium citrate 2 g/l as morganic salt with other basal components. The optimal pH of medium and fermentation temperature were 6.2 and $35^{\circ}C$, respectively. This strain required exclusively riboflavin and pantothenic acid for growth and bacteriocin production. In a 1l batch culture, stationary phase emerged after 8.5 hours of fermentation when 1.81 g/l of biomass was accumulated. The maximum antimicrobial activity was 3,894 IU/ml after 12 hours.

• Microbiology and Biotechnology Letters
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• v.24 no.2
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• pp.137-142
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• 1996

The biosynthesis and catabolite repression of cyclodextrin glucanotransferase(CGTase) and cyclodextrinase(CDase) were studied in Bacillus sp. KJI6. In accompanying to the cell growth, CGTase was synthesized during early growth phase (20h culture) and CDase was synthesized during late growth phase (60h culture). Synthesis of CGTase was rather constitutive than that of CDase in the absence or presence of carbon source. Production of CDase was strongly stimulated by amylopectin and $\gamma$-CD medium (about 6 times), but CGTase synthesis was slightly increased (about 1.3 times). Easily metabolizable carbohydrates such as D-glucose, D- fructose and D-mannose completely repressed the expression of CDase, whereas their repressive effect to CGTase synthesis was relatively negligible. By addition of 10 mM cAMP, any significant effect on the synthesis of the two enzymes was not observed. Hardly metabolizable glucose analogues such as 2-deoxy-D-glucose and 3-0-methyl-D-glucopyranose also did not show any repression on the syntheses of CGTase and CDase. This indicates that D-glucose has to be metabolized to exert its repressive effect. With these results, it seems likely that the biosynthesis of CGTase and CDase are regulated by the catabolite repression due to unknown metabolite(s) of EM pathway.