• Microbiology and Biotechnology Letters
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• v.17 no.2
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• pp.109-114
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• 1989

Seventeen bacterial strains producing an extracellular soybean milk clotting enzyme were Isolated from 150 soil samples, and identified as Bacillus cereus(8 strains), Bacillus pumilus(8 strains) and Bacillus licheniformis (1 strain). Among them, Bacillus pumilus strain 118 and Bacillus licheniformis strain 192 showed relatively high soybean milk clotting activity. The coagulability of enzymes from these strains decreased as the pH of soybean milk was increased from 6.0 to 7.0. The optimum temperature for soybean milk clotting activity was $65^{\circ}C$.

• KSBB Journal
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• v.24 no.6
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• pp.508-514
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• 2009

This study investigated the production of catalase from Bul-kyo soil bacteria through fermentation process. Isolation and selection of bacteria was performed through chemical and physiological analysis. Catalases were produced from bacteria which belong to 3 different species (Bacillaceae bacterium BKBChE-1, Bacillus sp. BKBChE-2, Bacillus flexus BKBChE-3) confirmed by using 16S rDNA sequence method. The catalases were found to be stable in the temperature range of $30^{\circ}C-60^{\circ}C$ for BKBChE-1, BKBChE-2 and BKBChE-3 and also in the pH range of 9.0-12.0 for BKBChE-1 and BKBChE-3. Long-term stability of the catalases was about 20 days at $4^{\circ}C$. However, BKBChE-2 has kept its activity over 30 days at $4^{\circ}C$.

• Applied Biological Chemistry
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• v.31 no.1
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• pp.79-85
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• 1988

The effects of herbicides on biochemical processes in soil environment were studied by examining the effects of the chemical structure of each herbicides on soil enzyme activities and pesticides residue revealed when soil treated with urea was incubated at $28{\pm}1^{\circ}C$ for 56 days. The inhibition effects of herbicides on soil enzyme activites in soil decreased in the order of urea group>dinoseb>propanil>diphenyl eter group>acid amide group for urease, and dinoseb>urea group>diphenyl ether group>acid amide group for L-glutaminase and protease, dinoseb>diphenyl ether group>urea group>acid amide group for phosphatase. Herbicides inhibited the activities of soil enzyme in the early stage of treatment but increased the activities of urease, L-glutaminase and protease in the late stage. When herbicides were treated in soil together with urea the degradation of insecticides was accelerated.

• Journal of the Korean Society of Food Science and Nutrition
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• v.38 no.6
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• pp.801-806
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• 2009

A species producing transglutaminase (EC 2.3.2.13) was isolated from forest soil and identified as Streptomyces platensis YK-2. The transglutaminase was purified from culture broth by 50% methanol precipitation, followed by successive chromatography on DEAE-Sephadex. The yield and purification-fold was 63.4% and 2.2-fold, respectively. The purified microbial transglutaminase (MTG) migrated as a single band of approximately 45 kDa upon sodium dodecyl sulfate polyacrylamide gel eletrophoresis. The isoelectric point determined by multichambered electrofocusing was pH $6.0{\sim}7.0$. The enzyme was strongly inhibited by $Hg^{++}$, but was activated by $Cd^{++}$, $Mg^{++}$, $Mn^{++}$, $Pb^{++}$ and reducing agents such as dithiothreitol and mercaptoethanol.

• Korean Journal of Microbiology
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• v.40 no.2
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• pp.139-146
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• 2004

A bacterium producing alkaline cellulase was isolated from soil, leaf mold and compost, and was identified as alkalophilic Bacillus sp. HSH-810 by morphological, cultural and biochemical determination. The optimum cul-ture condition of Bacillus sp. HSH-810 for the growth and alkaline cellulase production was $30^{\circ}C$ and pH 10.0. The maximum alkaline cellulase production was obtained when 1.0%(w/v) CMC, 0.5%(w/v) peptone, 0.02%(w/v) $CaCl_2$ and 0.02(w/v) $CoCl_2$ were used as carbon source, nitrogen source and mineral source, respectively. The optimum pH and temperature of the enzyme activity were pH 10.5 and $50^{\circ}C$, respectively. This enzyme was fairly stable in the pH range of 6.0-13.0 and at $50^{\circ}C$. For the effect of surfactants, the activity of alkaline cellulase was stable in the presence of sodium-$\alpha$-olefin sulfonate (AOS), sodium dodecyl sulfonate (SDS), Tween 20 and Tween 80, but inhibited by the presence of 0.1 linear alkyl-benzene sulfonate (LAS) sig-nificantly.

• Journal of the Korean Society of Food Science and Nutrition
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• v.37 no.11
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• pp.1507-1514
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• 2008

Cholesterol oxidase catalyses the conversion of cholesterol to 4-cholesten-3-one. This enzyme has been used for clinical assay of human serum cholesterol and for reduction of cholesterol level in foods and feeds. In order to search the microorganism which has a high extracellular and stable activity of cholesterol oxidase, soil microorganisms were screened. As a result, the one with the highest extracellular cholesterol oxidase activity was obtained and named as the BEN 115. The BEN 115 strain was identified as one of the Nocardia species based on our taxonomic studies. The cholesterol oxidase from this strain was shown to have two bands of extracellular proteins on SDS-PAGE and Western blot. Their molecular masses were estimated to be about 55 and 57 kDa, respectively. In addition, this cholesterol oxidase was considerably stable at the broad range of pH $3.5{\sim}9.5$ and at the temperature of $25{\sim}55^{\circ}C$. The optimum pH and temperature of this cholesterol oxidase were pH 5.5 and $35^{\circ}C$, respectively. The activity of extracellular cholesterol oxidase could be enhanced 1.6 to 2.0 folds by the addition of nonionic detergent such as Triton X-114, Triton X-100, or Tween-80 into the culturing broth. The substrate specificities against campesterol, sitosterol and stigmasterol were measured to be 50%, 50%, and 27%, respectively, compared to the cholesterol. These results suggest that Nocardia sp. BEN 115 may be useful as a microbial source of cholesterol oxidase production.

• Microbiology and Biotechnology Letters
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• v.31 no.2
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• pp.157-164
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• 2003

An alkali-tolerant bacterium producing the xylanase was isolated from soil and identified as Bacillus alcaiophilus. This strain, named B. alcalophilus AX2000, was able to grow and produce xylanase optimally at pH 10.5 and $37^{\circ}C$. The maximum xylanase production was obtained when 0.5%(w/v) birchwood xylan and 0.5%(w/v) polypeptone and yeast extract were used as carbon source and nitrogen source, respectively. The biosynthesis of xylanase was under the catabolite repression by glucose in the culture medium, and inhibited in the presence of high concentration of xylose. The maximum activity of xylanase was observed at pH 10.0 and $50^{\circ}C$ and the enzyme activity remained was over 80% at $60^{\circ}C$ and from pH 5.0 to 11.0.

• Proceedings of the Plant Resources Society of Korea Conference
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• 2007.11a
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• pp.343.1-343.1
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• 2007

• Korean Journal of Microbiology
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• v.32 no.4
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• pp.297-300
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• 1994

About thirty bacterial strains of actinomycete isolated from the soil were examined for the presence of restriction endonuclease activity. Streptomyces diastatochromogenes, which was identified previously, was found to contain restriction endonuclease activity. The purification of this enzyme, SdiI, was carried out via streptomycin sulfate precipitation and ammonium sulfate fractionation followed by hydroxylapatite column chromatography. Sephacryl S-200 HR column chromatography and second hydroxylapatite column chromatography. SDS-polyacrylamide gel electrophoresis of the active protein (purified from various column chromatography) resulted in 35,000 Da protein.

• Applied Biological Chemistry
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• v.38 no.6
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• pp.502-506
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• 1995

A Bacillus strain which produces ${\beta}-galactosidase$ with high transgalactosylation activity, was isolated from soil and tentatively designated as Bacillus sp. A1. When ${\beta}-galactosidase$ from Bacillus sp. A1 reacted with 40% (w/w) lactose, transgalactosylation ratio reached up to 90% at the 70% conversion of the initial lactose. The biosynthesis of the enzyme in Bacillus sp. A1 required lactose as an inducer and was repressed by glucose. Observing that the addition of amino acids to culture medium resulted in enhancing, to a significant extent, both the growth and the enzyme production of the strain, yeast extract and commercially available hydrolysates of protein were examined for the suitability as amino acid source. As it turned out, SMP, an enzymatic hydrolysis product of soybean protein from Fuji Oil Co.(Japan), was the most suitable for optimization of the culture medium. When Bacillus sp. A1 was cultured in the presence of 0.5% SMP and 2% lactose, the enzyme activity increased up to $1.8\;U/m{\ell}-broth$.