• Bulletin of Food Technology
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• v.23 no.4
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• pp.544-551
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• 2010

식품산업에서 박테리오파아지를 첫째, 동물 보건에서 항생제 대체품으로서, 둘째, 식품에서 바이오보존제(biopreservative)로서, 셋째, 식품 체인에서 병원성 세균을 검출하기위한 도구로서 다양하게 이용하고자 최근에 널리 인지하고 있다. 박테리오파아지는 바이러스로서 세균을 감염시키고 용해하는 특성이 있으며, 식품 안전과 관련하여, 1) 포유 동물세포에 무해하여 박테리오파아지를 안전하게 이용할 가능성, 2) 발효식품에 적절한 스타터 역할을 하거나 천연 미생물균총을 그대로 보존하는 박테리오파아지의 높은 숙주 선택성이라는 2가지 특징을 지니고 있다. 최근에는 식품첨가물로서 박테리오파아지를 '먹을 수 있는 바이러스'로 인정할 수 있을지 논의되고 있다. 식품유래 병원성 세균을 제어하기 위한 파아지의 이용가능성과 생물학 분야에서 관련되는 기초연구를 하고자 할 때 생기는 제한점 등에 대해서 고찰하고자 한다.

• Korean Journal of Poultry Science
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• v.37 no.3
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• pp.283-287
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• 2010

In the present study we report in vivo inhibitory potential of single strain of bacteriophage ($CJ{\phi}07$) in day-old SPF chicks experimentally infected with Salmonella enteritidis (SE). The bacteriophages prepared by feed additives and drinking water were given to chicks for 20 days starting prior 10 days before challenge with SE. Chicks were euthanized at 10 days after challenge for quantitative salmonella isolation from intestine and determination of environmental contamination level of salmonella. Bacteriophage therapy as additives in feed and drinking water resulted in significant inhibition of the SE replication in intestines of SPF chickens (P<0.05). In addition, environmental contamination by SE fecal shedding was decreased in bacteriophage-treated birds. Therefore, bacteriophage $CJ{\phi}07$ examined in this study may be a plausible alternative to antibiotics for the reduction of salmonella infection both in poultry.

• Korean Journal of Microbiology
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• v.39 no.4
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• pp.277-282
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• 2003

Bacteriophage P4 ost2 which is the P4 mutant suppressing sir mutations of Bacteriophage P2, was isolated as a plaque-former by plating P4 ash8 sid 71 kmr intS on the lawn of P2 sir3 lysogen. P4 ost2 turned out to be the P4 mutant suppressing sir mutations of P2 in one-step growth experiments.

• KOREAN POULTRY JOURNAL
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• v.43 no.5
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• pp.136-137
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• 2011

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2002.05a
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• pp.523-524
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• 2002

• KSBB Journal
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• v.10 no.5
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• pp.533-539
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• 1995

An autolytic system based on a thermally inducible phage lambda, λHL1, has been applied for the recovery of poly(3-hydroxybutyrate) [PHB] from a recombinant Escherichia coli XL1-Blue, harbouring a plasmid (pSYL105) containing the Alcaligenes eutrophus PHB biosynthesis genes. The lytic capability ofλHL1 was evaluated in flask culture for both lysogens, XL1-Blue (λHL1) and XL1-Blue (λHL1, pSYL105). When the optical density of culture at 600nm(OD600) reached 0.2, cell lysis was induced by increasing the temperature from $30^{\circ}C$ to $42^{\circ}C$. Most cells of XL1-Blue ($\lambda$HL1) were lysed by the autolytic system in an hour after the thermal induction, while the lytic efficiency was slightly lower for XLl-Blue (λHL1, pSYL105). The existence of pSYL105 in cells seemed to inhibit, to some extent, the lytic capability of λHL1 even at low PHB content. The lylic efficiency remarkably decreased as the induction was delayed to allow PHB accumulation. When a chemical induction using 2% (v/v) chloroform was introduced after an hours of thermal induction, we could obtain a good lytic efficiency.

• Korean Journal of Microbiology
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• v.42 no.1
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• pp.62-66
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• 2006

To study the packaging mechanism of the bacteriophage P2-P4 system which is a useful experimental tool for the study of viral capsid assembly, we analyzed the DNA contents of P4 sid- mutant, P4 ash8 sid71's phage particles. Two kind of particles having different density were separated by the CsCl buoyant equilibrium density gradient experiment with fresh made stock of P4 ash8 sid71. The DNA from each particles was prepared and its conformations was analyzed by electrophoresis. Unexpectedly, both particles contain not only dimeric and trimeric but also monomeric P4 DNA.

• KOREAN POULTRY JOURNAL
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• v.43 no.6
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• pp.145-148
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• 2011

• Korean Journal of Microbiology
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• v.24 no.2
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• pp.161-167
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• 1986

Some of the physiological properties of Sp816 bacteriophage of Bacillus subtilis SNU816 were characterized. It could form plaques on either B. subtilis SNU816 or B. natto 8102, but not on any other bacillus strains investrgated. Its plaque morphology was circular with a diameter of less than 1.0mm and had a narrow halo surrounding the clear center. Its latent period was 34-36 min and had a burst size of 547. It was most stable at pH 6.0, and rapidly inactivated at $60^{\circ}C$ with a initial deaty rate of -0.216 $min^{-1}$. Host range, thermal inactivation rate at $60^{\circ}C$, pH stability, and UV sensitivity revealed that SP816 was quite different from any other phages investigated together but seemed to be rather related to B. natto phages.

• YAKHAK HOEJI
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• v.47 no.3
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• pp.176-179
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• 2003

A library of unlimited number of novel lectins with diverse specificities has been previously generated by randomly mutating the carbohydrate-recognition domain of Maackia amurensis hemagglutinin (MAH). To establish the experimental environment capable of selecting high affinity mutant lectins in E. coli, phage display system was adapted. Carbohydrate binding capacity of two phagemid vectors, pComb3 and pComb8 displaying wild-type MAH lectin was assessed. Specific bindings of pComb3 and pComb8 phages expressing w.t. MAH to affinity-purified polyclonal anti-MAH antibody and to glycophorin was demonstrated. Both phages also showed strong hemagglutinating activity to intact but not sialidase-treated human erythrocytes, which is consistent to the specificity of native MAH. Taken together, two different phage display vectors successfully allowed the expression of active MAH as a fusion protein on the surface of bacteriophage, which will lead to preparation of unique plant lectins with high affinity toward a variety of carbohydrate chains.