• 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.

• Journal of environmental and Sanitary engineering
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• v.13 no.3
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• pp.113-120
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• 1998

For a microbial control of a plant pathogenic Pseudomonas syringae, Bacillus sp. strain BT182-3 was isolated. The strain BT182-3 had a growth inhibition against P. syringae not only on agar plate but also on cultured broth. After heat treatment at $40^{\cird}C$ and $80^{\cird}C$ for 30min, the lytic substance from the strain BT182-3 had about 52% remaining activity and 17% remaining activity, respectively. The optimal pH and temperature of the lytic substance was 6.0 and $28^{\cird}C$, respectively. Germination ratio of healthy radish seeds was 87% at $25^{\cird}C$ for 5 days in 0.8% saline, and that of the radish seeds infected with P. syringae was 67%, while that of the radish seeds treated with cultured broth of the strain BT182-3 was 90%. The 5-days healthy radish seedlings were 3.90cm at high and the seedlings infected with P. syringae were 3.06cm at high, while the seedlings treated with cultured broth of the strain BT182-3 were 4.30cm at high. The growth of the radish seedlings infected with P. syringae was inhibited after cultivation for 40days on pots, while the growth of the infected radish seedlings with P. syringae was recovered at stem length, root length and total weight at the same as the healthy seedlings after treatment of a lytic substance from the strain BT182-3.

• Microbiology and Biotechnology Letters
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• v.24 no.2
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• pp.143-148
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• 1996

Thousand actinomycetes and 50 soil samples were used for the isolation of microorganisms producing yeast cell wall lytic enzymes. Among 493 strains producing large clear zones on autolysed washed yeast (AWY), 117 strains were selected on living yeast cell agar plates. With the method of lytic activity, one strain (St-1702) was selected, which was temporarily identified as Streptomyces eurythermus. The optimal condition for enzyme production of this strain was partially determined as follows: incubation of the strain for 3 days at 30$\circ$C in the medium containing 2% freeze dried yeast cell, 1% glucose, 1% K$_{2}$HPO$_{4}$, 0.01% MgSO$_{4}$'7H$_{2}$O, 0.5% peptone, and 0.2% (NH$_{4}$)$_{2}$CO$_{3}$ with pH 7.0. The protoplast formation of yeast by using the enzyme produced by this strain was compared with commercial enzymes.

• Journal of Microbiology and Biotechnology
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• v.28 no.11
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• pp.1946-1954
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• 2018

The aim of this study was to isolate and characterize a lytic Yersinia enterocolitica-specific phage (KFS-YE) as a biocontrol agent. KFS-YE was isolated and purified with the final concentration of ($11.72{\pm}0.03$) log PFU/ml from poultry. As observed by transmission electron microscopy, KFS-YE consisted of an icosahedral head and a contractile tail, and was classified in the Myoviridae family. KFS-YE showed excellent narrow specificity against Y. enterocolitica only. Its lytic activity was stable at wide ranges of pH (4-11) and temperature ($4-50^{\circ}C$). The latent period and burst size of KFS-YE were determined to be 45 min and 38 PFU/cell, respectively. KFS-YE showed relatively robust storage stability at -20, 4, and $22^{\circ}C$ for 40 weeks. KFS-YE demonstrated a bactericidal effect in vitro against Y. enterocolitica and provided excellent efficiency with a multiplicity of infection as low as 0.01. This study demonstrated the excellent specificity, stability, and efficacy of KFS-YE as a novel biocontrol agent. KFS-YE may be employed as a practical and promising biocontrol agent against Y. enterocolitica in food.

• Korean Journal of Environmental Biology
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• v.22 no.1
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• pp.184-191
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• 2004

To investigate bacteria with algalytic activities against Anabaena cylindrica when water blooming occurs and to study enzyme profiles associated with alga-lytic activity, various bacterial strains were isolated from surface waters and sediments in eutrophic lakes or reservoirs in Korea. Among 178 isolates, only nine isolates exhibited lytic abilities against A cylindrica on the agar plates, and then the isolate AK-13 was selected as the strongest in lysing the cyanobacterium A. cytindrica. The strain AK-13 was characterized and identified as Sinorhizobium sp. based on fatty acid methyl ether profiles and 16S rDNA sequence. According to the results of the enzyme assays, in the strain An-13 of Sinorhizobium sp., alginase, amylase, proteinase (caseinase and gelatinase), carboxymethyl-cellulase (CMCase), laminarinase, and lipase was produced, namely CMCase, laminarinase and protease were highly active. None of glycosidase was produced. Therefore, enzyme systems of Sinorhizobium sp. AK-13 were very complex to degrade cell walls of A. cylindrica. The peptidoglycans of A. cylindrica mat be hydrolyzed and metabolized to a range of easily utilizable monosaccharides or other low molecular weight organic substances by Sinorhizobium sp. AK-13.

• Korean Journal of Microbiology
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• v.40 no.2
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• pp.115-120
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• 2004

A Gram (-), rod-shaped bacterium in size of 1.3∼$1.8{\times}0.35{\mu}m$ inhibiting the growth of cyanobacterium (Ana-baena cylindrica) was isolated and designated NG-2 in this manuscript. This isolate showed positive reactions for catalase and oxidase, and optimal growth conditions of 35∼TEX>$40<^{\circ}C$ and pH 9.0. In a mixed-culture of A. cylindrica and the isolate, each microorganism grew inverse-proportionally, and the cyanobacterial vegetative cells almost completely disappeared within 24 hours. NG-2 lysed A. cylindrica only under light, which means that lytic activity of NG-2 was dependent on the photosynthetic activity of host. When observed under phase contrast microscope, the isolate lysed vegetative cells of A. cylindrica in scattered state in a liquid medium, whereas het-erocysts have not been lysed. When cyanobacterial cell walls have been lysed partly, NG-2 attatched around A. cylindrica filament and formed colony, then encouraged complete lysis of cyanobacterial cells. The isolate showed similar lytic activity in natural water as in an artificial medium. And lytic activity of NG-2 was enhanced when attached on expandable polystyrene bead.

• Journal of Microbiology and Biotechnology
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• v.28 no.9
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• pp.1542-1546
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• 2018

Bacterial canker in kiwifruit is caused by Pseudomonas syringae pv. actinidiae (Psa). In this study, the bacteriophage PPPL-1 effective against Psa was characterized. Belonging to the Podoviridae family, PPPL-1 was effective against most Psa strains as well as most Pseudomonas syringae pathovars. PPPL-1 carries a 41,149-bp genome with 49 protein coding sequences and is homologous to the previously reported phiPSA2 bacteriophage. The lytic activity of PPPL-1 was stable up to $40^{\circ}C$, within a range of pH 3-11 and under 365 nm UV light. These results indicate that the bacteriophage PPPL-1 might be useful to control Psa in the kiwifruit field.

• Animal cells and systems
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• v.11 no.2
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• pp.175-182
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• 2007

The lysozyme II gene of cabbage butterfly Artogeia rapae was cloned from fat body of the larvae injected with E. coli and its nucleotide sequence was determined by the RACE-PCR. It has an open reading frame of 414 bp nucleotides corresponding to 138 amino acids including a signal sequence of 18 amino acids. The estimated molecular weight and the isoelectric point of the lysozyme II without the signal peptide were 13,649.38 Da and 9.11, respectively. The A. rapae lysozyme II (ARL II) showed the highest identity (81%) in the amino acid sequence to Manduca sexta lysozyme among other lepidopteran species. The two catalytic residues ($Glu^{32}$ and $Asp^{50}$) and the eight Cys residue motifs, which are highly conserved among other c-type lysozymes in invertebrates and vertebrates, are also completely conserved. A phylogenetic analysis based on amino acid sequences indicated that the ARL II was more closely related to M. sexta, Hyphantria cunea, Heliothis virescens, and Trichoplusia ni lysozymes. The ARL II gene was expressed in Spodoptera frugiperda 21 insect cells and the recombinant ARL II (rARL II) was purified from cell-conditioned media by cation exchange column chromatography and reverse phase FPLC. The purified rARL II was able to form a clear zone in lysoplate assay against Micrococcus luteus. The lytic activity was estimated to be 511.41 U/mg, 1.53 times higher than that of the chicken lysozyme. The optimum temperature for the lytic activity of the rARL II was $50^{\circ}C$, the temperature dependency of the absolute lytic activity of rARL II was higher than that of the chicken lysozyme at low temperatures under $65^{\circ}C$.

• Microbiology and Biotechnology Letters
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• v.11 no.1
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• pp.1-4
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• 1983

In order to determine a proper amount of sodium pyrophosphate (SPP) which protect Lactobacilli from phage attack, Lactobacillus casei YIT-9018 was grown in $Ca^{＋＋}$ free Murata medium having various concentrations of SPP after infections with phage Jl at different multiplicities of infection (MOI). it was found that the level of SPP to inhibit phage activity depended upon the level of MOIs. When the bacteria were infected by less than 10$^{-1}$ of MOI, 0.15% of SPP was sufficient, while with 10$^{0}$ of MOI, 0.175% of SPP was needed to inhibit the lytic activity completely.

• 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.