• Journal of Life Science
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• v.11 no.2
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• pp.92-93
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• 2001

Bacillus sp. KYJ 963, which was isolated from Korean salt-fermented anchovy (anchovy-jeot), produces an extracellular ${\beta}$-amylase. The analysis of the digestion products of substrates by thin layer chromatography from the purified protein revealed that the enzyme could not hydrolyze maltose or ${\alpha}$-cyclodextrin. In the amino acid composition analysis, the major characteristic of the ${\beta}$-amylase was the high proportion of amino acids that possess short side chain such as glycine and alanine.

• Microbiology and Biotechnology Letters
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• v.28 no.1
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• pp.59-61
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• 2000

The various extracellular enzymes produced by lactic acid bacteria isolated from kimchi were assayed to improve the shelf-life of kimchi. Peroxidase was not detected in all tested lactic acid bacteria and small amount of ascorbic acid oxidase was detected in Pediococcus pentosaceus and Lactobacillus brevis. In case of $\alpha$-amylase, 27.8 and 20.9 unit/mg were shown in Pediococcus acidilactici and Pediococcus pentosaceus, respectively but $\beta$-amylase and protease activities were very low. The enzyme related to textural property of kimchi, pectinesterase showed low activity but polygalacturonase activity was 0.28 unit/mg in Lactobacillus homohiochii and 0.27 unit/mg in Lactobacillus plantarum.

• Journal of the Korean Wood Science and Technology
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• v.19 no.2
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• pp.22-29
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• 1991

The endo-1,4-${\beta}$-xylanase was extracted and purified from the extracellular xylanolytic systems of Trichoderma viride. The crude enzyme was chromatographed with ion-exchange reins of DEAE Sepharose CL-6B, Sepharose, S-Sepharose CL-6B and the resulting xylanase was turned out to be a single protein as 20KD hy SDS-polyacrylamide gel electrophoresis. The xylooligomers were obtained from xylan by incubation with the purified xylanase up to 50%. The ${\beta}$-xylosidase lost its activity completely by incubation of crude enzyme for 24hr with buffer solution of pH 2.8 at $27^{\circ}C$. And also, the xylooligomers were obtained from xylan as a main product by incubation with the crude enzyme treated with acidic buffer.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1998.11a
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• pp.161-161
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• 1998

To achieve the aim of this investigation, the extracellular protease was isolated from bacteria BAC-4, a strain was cultivated in the medium for the production of penicillin acilase in a period of 32 hours. The enzyme was first purified by aceton precipitation method, followed by ion exchange chromatography on DEAE-sephacel column. The highest specific activity of the aceton fraction was found to be 2.19 unit per mg, with degree of purification of 13 times. Further purification of the enzyme on DEAE -sephacel had a specific activity of 58.6 unit per mg and degree of purification of 344 times compared to its crude extract. The optimum pH of the enzyme was 8.4, and the potimum temparature was 37$^{\circ}C$. The K$\_$M/ and $V_{max}$ calculated at experiment conditions were found to be 0.66%(W/V) and 3.61 unit per mL respectively.

• Korean Journal of Microbiology
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• v.30 no.6
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• pp.507-513
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• 1992

Serratia marecescens RH1 isolated from soil samples produced large amount of extracellular proteases. One of the genes encoding an extracellular protease form S. marcescens RH1 was cloned in Escherichia coli by shot gun cloning method. The cloned protease, SSP, was stably expressed by its own promoter and excreted into the extracellular medium from E. coli host (ORF) of 3.135 nucleotides corresponding to 1.045 amino acids (112 kDa). The nucleotide and deduced amino acid sequence of SSP showed high overall homology (88%) to one of the S. marcescens protease (27), but low homology to other serine protease families. The optimal pH and temperature of the enzyme were pH 9.0 and 45.deg.C respectively. The activity of protease was inhibited by phenylmethylsulfonyl fluoride (PMSF), which suggests that the enzyme is a serine protease.

• Journal of Microbiology and Biotechnology
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• v.17 no.5
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• pp.745-752
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• 2007

A $\beta$-glucosidase from the algal lytic bacterium Sinorhizobium kostiense AFK-13, grown in complex media containing cellobiose, was purified to homogeneity by successive ammonium sulfate precipitation, and anion-exchange and gel-filtration chromatographies. The enzyme was shown to be a monomeric protein with an apparent molecular mass of 52 kDa and isoelectric point of approximately 5.4. It was optimally active at pH 6.0 and $40^{\circ}C$ and possessed a specific activity of 260.4 U/mg of protein against $4-nitrophenyl-\beta-D-glucopyranoside$(pNPG). A temperature-stability analysis demonstrated that the enzyme was unstable at $50^{\circ}C$ and above. The enzyme did not require divalent cations for activity, and its activity was significantly suppressed by $Hg^{+2}\;and\;Ag^+$, whereas sodium dodecyl sulfate(SDS) and Triton X-100 moderately inhibited the enzyme to under 70% of its initial activity. In an algal lytic activity analysis, the growth of cyanobacteria, such as Anabaena flos-aquae, A. cylindrica, A. macrospora, Oscillatoria sancta, and Microcystis aeruginosa, was strongly inhibited by a treatment of 20 ppm/disc or 30 ppm/disc concentration of the enzyme.

• Korean Journal of Microbiology
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• v.22 no.4
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• pp.257-263
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• 1984

A strain producing an extracellular cytosine deaminase was isolated from soil samples. The enzyme obtained from the strain possessed the substrate specificity to both cytosine and 5-fluorocytosine. From the results of its morphological, cultural, physiological, and biochemical properties, the strain was thought to be the genus Arthrobacter. Therefore, it was named as Arthrobacter sp. JH-13. The composition of optimum medium for the enzyme formation was 0.5% of peptone, 0.5% of meat extract, 0.5% of soluble starch, and 0.1% of KCl. The optimum pH for the enzyme formation was 8.0. When the microoganism was cultured aerobically in the above medium, enzyme production reached at maximum in 54 hours at $30^{\circ}C$.

• The Korean Journal of Ecology
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• v.17 no.1
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• pp.79-90
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• 1994

Water samples were taken at 6 stations from the mouth of Keum River to Kogunsan Archipelago of West Sea during December, 1991 to August, 1992, to determine the distribution of heterotrophic bacteria, their biovolumes and heterotrophic activities. Heterotrophic marine bacteria ranged from $1.0\;{\times}\;10^3to\;5\;{\times}\;10^5c.f.u.$ /ml. As for morphological distribution measured by epifluorescence microscopy, rod-shaped bacteria were between 45% and 72% of all cells during investigation period. Average biovolume of sampled bacteria ranged from $(7.69\;{\pm}\;0.18)\;{\times}10^{-2}to\;(8.18\;{\pm}\;0.38)\;{\times}\;10^{-2}\;{\mu}m^3$ for coccoid bacteria, and from $(6.09\;{\pm}\;0.29)\;{\times}10^{-2}to\;(7.72\;{\pm}\;0.41)\;{\times}\;10^{-2}\;{\mu}m^3$ for rod-shaped ones. The activities of extracellular enzymes ranged from 0.01 to 2.6 ${\mu}M$ /l /hr for glucosidase, from 0.01 to 2.6 ${\mu}M$ /l /hr for amylase, from 0.01 to 8.86 ${\mu}M$ /I /hr phosphatase and from 0.01 to 0.94 ${\mu}M$ /l /hr for chitinase. Extracellular enzyme activities were higher in summer season than in other sampling periods, and phosphatase showed the highest activity among measured extracellular enzymes. Bacterial distribution and their extracellular enzyme activities were associated with water temperature and organic nutrients, but bacterial cell volumes showed no direct relationship with extracellular enzyme activities.

• Journal of Life Science
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• v.9 no.4
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• pp.489-492
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• 1999

A bacteial strain which can produce the extracellular fibrinolytic enzyme was isolated from Jeot-Gal (anchovy) that was Korean traditional salt-fermented fish. The isolated bacterium was identified to be a strain of Bacillus sp. The optimal medium for fibrinolytic enzyme production was determined to consist of 5 g maltose, 10 g defatted soybean, 20 g sodium chloride, 1.75 g K2HPO4 per liter (pH 7.0)

• The Microorganisms and Industry
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• v.12 no.2
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• pp.36-39
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• 1986