• Korean Journal of Environmental Agriculture
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• v.27 no.3
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• pp.292-297
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• 2008

A bacterium, which was named to be Bacillus sp. E64-2, capable of degrading endosulfan was isolated from the environmental sample using enrichment culture technique. The Bacillus sp. E64-2 was able to degrade 99% of 10 mg/L endosulfan in the culture media within 7 days at $30^{\circ}C$. Endosulfan diol was the only intermediate by the endosulfan degrading bacterial culture and the pH value of the culture media was significantly increased to pH 8.4 from pH 7.0 after 7 days of incubation. When the endosulfan and the crude extract of the strain were incubated, endosulfan diol was a major metabolite. Both the enzymatic reaction and the pH-increasing effect contribute to the degradation of endosulfan by the bacterial culture.

• Journal of Life Science
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• v.19 no.10
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• pp.1424-1431
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• 2009

Shrimp Jeot-Gal is a popular traditional Korean fermented seafood and has been used for seasoning. We isolated a bacterium showing strong extra-cellular fibrinolysis and chitinase activity from shrimp Jeot-Gal and the strain was designated SC082. SC082 was identified as Bacillus licheniformis by 16S rRNA sequence homology search. B. licheniformis SC082 exhibited optimum temperature, pH, and salt concentration at $37^{\circ}C$, pH 7.0, and 6%, respectively. Substrate specificity of the culture supernatant from B. licheniformis SC082 was detected in fibrin, skim milk, and chitin plate. The fibrinolytic activity was highly maintained up to $50^{\circ}C$ at a pH of 7.0 for 3 hr and was stable up to pH 9.0 at $37^{\circ}C$ for 3 hr. The chitinase activity was remarkably induced by addition of 1.0% colloidal chitin and the pH and temperature optima of the enzyme were 5.0 and $45^{\circ}C$, respectively. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis and zymogram analysis, this strain produced three fibrinolytic isozymes and two chitinase isozymes. The approximate molecular weights of the putative fibrinolytic enzymes were 23.0, 62.0, and 72.0 kDa and those of the chitinases were 62.0 and 55.0 kDa, respectively. The antioxidant activity of SC082 was also measured by using 2,2-diphenyl-l-picryl-hydrazyl (DPPH) free radical. The DPPH radical scavenging was slightly increased in a dose-dependent manner.

• Journal of Animal Science and Technology
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• v.51 no.5
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• pp.387-394
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• 2009

This study was carried out to screen and identify the chitinase and chitosanase producing microorganisms from the feces of calves medicated DFM sincluding chitin in order to do the immune fortification of Korean Native calves. Ten isolates were grown in the medium containing chitin and chitosan that had more than $10^5$ cfu/g in feces. Among these 10 strains, 2 strains (HANDI 110 and HANDI 309) had the chitinase activities and 2 strains (HANWOO and HANYOO) had the chitosanase activities in calves' feces. They showed no reaction in hemolysis tests by utilizing chitin and chitosan. The results from morphological, physicochemical and genetical identification indicated the HANDI 110 as a strain of Escherichia fergusonii, HANDI 309 was identified as a strain of Acinetobacter parvus, HANWOO was identified as a strain of Comamonas koreensis, and HANYOO as a strain of Chryseobacterium indologenes.

• Korean Journal of Microbiology
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• v.54 no.1
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• pp.46-52
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• 2018

Biodegradation pathway of dibenzofuran (DBF) of Novosphingobium pentaromativorans US6-1, a high-molecular-weight polycyclic aromatic hydrocarbons degrading strain, was investigated via analysis of metabolic intermediates and transcriptome. As a result, 3(2H)-benzofuranone, a basic skeleton of the metabolic intermediates produced by lateral dioxygenation process, was detected as an intermediate. RNA-Seq analysis confirmed that most of the expressed genes upon exposure to DBF were related to the lateral degradation pathway. Based on these results, the biodegradation pathway of DBF by N. pentaromativorans US6-1 was proposed.

• Journal of the Korean Society of Food Science and Nutrition
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• v.42 no.4
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• pp.627-632
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• 2013

High levels of an extracellular phytase were isolated from kimchi and found to be produced from a bacterial strain of Lactobacillus sakei (designated as L. sakei Wikim001). Phytase activity was measured from liberated inorganic phosphate obtained by a modification of the ammonium molybdate method using brown rice. Phytase activity was also detected in the culture broth supernatant at the stationary phase. The highest levels of phytase activity from L. sakei Wikim001 were detected at pH 5.0~6.5 and $30{\sim}40^{\circ}C$.

• Food Science and Preservation
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• v.7 no.4
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• pp.414-417
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• 2000

Competent cell transformation of B. subtilis AC819 was carried out using phenotypic protease-defective(Npr-) DNA of B. subtilis MT-2. An obtained transformant, designated B. subtilis HL-1, was obtained by homologous DNA recombination. Phenotypes of B. subtilis HL-1 were characterized histidine requirement streptomycin-resistance, tetracyclin resistance and non-producing protease. Protoplast transformation frequency of B. subtilis HL-1 by plasmid pUB110 was higher than that of B. subtilis MT-2. From this result, B. subtilis HL-1 is useful for protease gene transformation and thermostable protease gene cloning as a host.

• The Korean Journal of Mycology
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• v.14 no.3
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• pp.189-194
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• 1986

The aim of this study was to investigate physiological chracteristics of Lentinus edodes in Korea. We tried to detect properties of the several wood-degradative enzymes and investigate patterns of the enzyme production. A specific carbon source was used in the enzyme induction media for each enzymes, and the crude extract was used for the enzyme solution. With these enzyme solution, we investigated optimum temperature and pH conditions of their reactions. Moreover we investigated transition patterns of the enzyme production of the several wood-degrad­ative enzmes from Complex and Saw dust media for the purpose of studying the mechanisms of the wood component degradation by this fungus. It was assumed that the order of the wood com­ponent degradation was cellulose, xylan, and then pectic substances, and that the synergistic effects of these substances also influenced the degradation of wood components.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1978.04a
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• pp.98.5-99
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• 1978

항생물질과 RNA 분해효소를 동시에 생산하는 방선균의 한 균주를 토양으로부터 분리하여 이 균주가 생산하는 RNA 분해효소의 물리화학적 성질 및 분해산물에 대해 검토하였다. 효소반응의 최적 pH 및 온도는 명명 pH 5.6과 $50^{\circ}C이었다.$ $37^{\circ}C$ 에서 90분간 열처리 시켰을 때, 이 효소의 활성은 비교적 안정하였지마는 $50^{\circ}C$ 에서 90분간 열처리 시켰을 때는 효소활성이 심하게 저하되었다. 이 효소의 활성은 $Ba^{2+}$ 에 의하여 50% 정도의 저해 작용을 나타내었지만 EDTA에 의해서는 저해되지 않았다. 이 효소에 의한 RNA분해로 이 효소가 대사산물로서 guanosine, adenosine과 밝혀지지 않은 두 가지의 핵산관연물질을 생산함을 알 수 있었다. 제2보에서는 ENase의 효소학적 성질을 검토하였으며 이후 항생물질 측면에서 검토할 예정이다.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1992.05a
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• pp.22-22
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• 1992

국내의 토양에서 Streptomyces spp.를 분리하였고 이 중 항균활성이 우수한 균주들을 선별하였다. 이들 균주들을 적절한 조건에서 배양하여 얻은 배양액을 이온 교한 수지와 흡착 크로마토그래피를 행하여 항생물질들을 분리하였다. 이들 항생물질들은 Bacillus subtilis, Pyricularia oryzae, Alternaria mail, Candida albicans, Mycobacterium smegmatis, Pseudomonas aeruginosa , 및 Escherichia coli에 강한 항균활성을 나타내었다. 각 항생물질들을 산으로 가수분해하고 흡착관 크로마토그래피로 가수분해 생성물을 분리하였다. 분리한 항생물질과 가수분해 생성물들의 $^1$IH-NMR, $13^{C}$ -NMR, FAB-Mass 스펙트럼을 분석하여 구조를 연구하였다.

• Microbiology and Biotechnology Letters
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• v.45 no.2
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• pp.143-148
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• 2017

Ten Bacillus strains possessing amine oxidase activity were selected from 126 Bacillus isolates from meju and doenjang (two traditional Korean soybean foods). Among the isolates, two B. licheniformis strains (8MI05 and 8MS03) harbored the amine oxidase gene yobN. By conducting a gene search against published B. licheniformis genomes, the possession of yobN was proved to be a strain-specific property. Both strains degraded four types of biogenic amines (cadaverine, histamine, putrescine, and tyramine) supplemented in tryptic soy broth during their culture. A recombinant harboring yobN also degraded the four types of biogenic amines during cultivation. Both Bacillus strains could grow at a NaCl concentration of 14% and exhibited strain-specific protease and lipase activities.