• 대한미생물학회지
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• 제20권1호
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• pp.55-63
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• 1985

Phosphate, ammonia, glucosamine, glucose, pyruvate, succinate, fumarate, malate and acetate were examined for their ability to control the heat-stable enterotoxin (ST) production in succinate salts medium or in M9 medium. The results obtained were summerized as follows. 1. When the initial phosphate concentration was adjusted to 1.0mM, ST production was decreased to 80u/ml or less. But when the initial phosphate concentration was adjusted to 64mM or 100mM, enterotoxin production was 320u/ml. 2. When the initial ammonia concentration in the medium was adjusted to 1.0mM, no ST production and cell growth were observed. But when ammonia concentration was adjusted to 10mM, 19mM, 38mM or 76mM, enterotoxin production was 320u/ml. 3. Among carbon sources, glucosamine, glucose, pyruvate, succinate, fumarate, malate and acetate, acetate supported the highest specific production (928 unit/O.D.) of heat-stable enterotoxin. From this results, we could assume that heat-stable enterotoxin production is controlled by stringent control mechanism. 4. When the pH of the succinate salts medium was kept between 6.2 to 6.5, no heat-stable enterotoxin production was observed, but when the pH of the medium was kept between pH 6.2 to 6.5, 267 unit/O.D. of heat-stable enterotoxin was produced. 5. Glucose inhibited the heat-stable enterotoxin production and the mechanism was assumed due to its capacity to lower the pH of the medium during catabolysis and its high metabolic energy.

• 약학회지
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• 제30권5호
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• pp.228-231
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• 1986

The effect of temperature and pH on the degrdation of minoxidil in the aqueous solution was investigated and the stability of pharmaceutical preparation for solution was also studied. The degradation of minoxidil in the aqueous solution was first order type reaction and the rate constant at $20^{\circ}C$ in pH 7.0 phosphate buffer solution was 9.464${\times]10^{-3} day^{-1}$ and calculated activation energy was 11.7 kcal/mol. The degradation of minoxidil was acid-base catalytic reaction and the most stable range of pH was about 5.0. The liquid pharmaceutical preparation was very stable in 3 months.

• 한국미생물·생명공학회지
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• 제14권6호
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• pp.441-446
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• 1986

Pseudomonas synxantha A3가 생산하는 세포외 guanine deaminase의 몇가지 성질을 검토하였다. 본 효소의 안정 pH는 6.5-7.5 부근이었으며, 열안정성을 검토하기 위하여 각 온도에서 10분간 처리하였을 때 4$0^{\circ}C$까지 안정하였고 그 이상의 온도에서는 서서히 실활되었다. 또한 pH 8.0의 0.2M potassium phosphate 완충액에 본 효소를 보관하였을 때 실온에서 30일간 안정하였고 alcohol 및 acetone은 본 효소의 안정화에 효과가 없었다. 효소활성을 위한 최적온도 및 pH는 각각 5$0^{\circ}C$와 pH 7-8 부근이었다. 본 효소는 1mM의 Hg$^{++}$, Ag$^+$, Li$^+$에 의해 각각 50%이상 저해되었으며, 0.1mM의 Ag$^+$에 의해서도50%이상 저해되었다. Li$^+$에 의해 저해된 본 효소에 EDTA를 가하였을 때 효소의 활성회복에 효과가 있었다. 본 효소의 활성은 1mM의 pentachlorophenol에 의해 50%, p-CMB에 의해 40%정도 저해되었다. p-CMB에 의해 저해된 본 효소에 thiol compound를 가하였을 때에는, 사용된 시약 중 glutathione이 본 효소의 활성회복에 효과적인 것으로 나타났다.

• 한국물환경학회지
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• 제27권4호
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• pp.438-444
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• 2011

Magnesium is one of the abundant natural resources in the earth crust and seawater, which is directly related to various organisms activities interconnecting with water-rock system. In aqueous system, magnesium is known to predominantly exist in the form of $Mg^{2+}$ ion which is verified in its $E_h-pH$ diagram. When it is at equilibrium in aqueous system, temperature takes an essential role to complete equilibrium states. This study represents the change of the stable region of magnesium ion according to temperature, and how the consequences would affect aquatic organisms. It was revealed that there is a noticeable tendency shrinking the stable region of magnesium ion in a diagram as temperature increases, and as a result, aquatic bio-species presumably have difficulties to absorb the nutrient. Also, it was considered that the water system would be acidified by decreasing alkalinity.

• 대한화학회지
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• 제54권3호
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• pp.275-282
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• 2010

분자 내 수소결합 가능성을 가지고 있는 2-fluorocyclopropanemethanol과 2-chlorocyclopropanemethanol에 대하여 MP2/6-311++G(d,p) 방법과 B3LYP/6-311++G(d,p) 방법으로 최적화 계산을 수행하였다. 두 분자 모두 가장 안정한 conformer에서 O-H의 수소가 F나 Cl을 향하고 있어 수소결합 가능성을 보이기는 하나 $H{\cdots}F$, $H{\cdots}Cl$ 거리가 van der Waals radii보다 커서 강한 수소결합이라 보기 힘들고 두 번째 안정한 conformer의 경우가 가까운 $H{\cdots}F$, $H{\cdots}Cl$ 거리를 보이며 더 강한 수소결합 가능성을 보였다. 그러나 에너지가 5 ~ 7 kJ 더 높게 나타났다. Methanol group과 F나 Cl이 서로 반대 방향을 향할 때 일반적으로 안정하나 앞의 가장 안정한 conformer보다는 에너지가 높다.

• 한국미생물·생명공학회지
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• 제19권4호
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• pp.383-389
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• 1991

저온에서 높은 활성을 나타내는 알칼리성 protease를 생산하기 위하여 여러가지 시료로부터 집적배양에 의해 저온성 세균을 분리하였다. 분리된 세균은 저온.알칼리성 Pseudomonas sp.인 것으로 판명되었으며, 효소생산을 위한 균생육의 최적 pH는 10.0, 온도 $20^{\circ}C$에서 4일간 배양하였을 때였다. 이 효소 활성의 최적 pH 및 온도는 각각 pH 10.5 및 $40^{\circ}C$였으며, pH 및 열안정성은 각각 pH 7.0~13.0, 온도 $50^{\circ}C$이하의 범위에서 비교적 안정하였다.

• Journal of Microbiology and Biotechnology
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• 제23권6호
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• pp.872-877
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• 2013

In a previous study, we isolated and reported a second species of the Saccharophagus genus, Saccharophagus sp. strain Myt-1. In the present study, an alginate lyase gene (algMytC) from the genomic DNA of Myt-1 was cloned and characterized. The DNA sequence fragment obtained contained an open reading frame of 1,032 bp that encoded a protein of 343 amino acids with an estimated molecular mass of 37.6 kDa and a pI of 6.60. The deduced protein, AlgMytC, had the conserved amino acid sequences (RTELREM, QIH, YFKAGVYNQ) of the polysaccharide lyase family 7. A BLAST homology search indicated that AlgMytC shared an amino acid sequence identity of 95.9% with alg7A of S. degradans 2-40. The cloned and purified AlgMytC protein showed optimal activity at $40^{\circ}C$, and retained more than 90% of its total activity even after treatment at $25^{\circ}C$ for 24 h. AlgMytC was very alkaliphilic with an optimal pH of 9.0, and more than 90% of its activity was retained in the pH range 8.5-10.0. Moreover, AlgMytC was stable over a wide pH range. The activity of AlgMytC was also stable in the presence of various detergents.

• 한국식품영양학회지
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• 제7권1호
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• pp.16-22
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• 1994

Xylanase from Bacillus sp. GS was purified through acetone precipitation, DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-100 gel filtration. The optimum reaction temperature of purified xylanase was 50t . Its optimum pH was between pH 6.0 and pH 6.5. This enzyme was stable below 5$0^{\circ}C$ for several hours and stable at between pH 5.5 and pH 8.0. The enzyme activity of xylanase was remarkably increased by Co++ and Cu++ ions. According to the study of hydrolysis mode of this enzyme, it was turned out to be ends type xylanase that can produce xylooligosaccharides, known as bifidogenic factor, from xylan.

• 한국미생물·생명공학회지
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• 제23권3호
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• pp.304-310
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• 1995

A thermophilic bacterium producing the extracellular cellulase-free xylanase was isolated from soil and has been identified as Bacillus sp. The optimal growth temperature was 50$\circ$C and the optimal pH, 7.0. Under the optimal growth condition, maximal xylanase production was 2.2 units/ml in the flask culture. The enzyme production was induced by xylan and xylose, but was repressed by sucrose or trehalose. The partially purified xylanase was most active at 70$\circ$C. It was found that the enzyme was stable at 65$\circ$C for 10 hours with over 75% of the activity. The enzyme was most active at pH 7.0 and retained 90% of its maximum activity between pH 5.0 and pH 9.0 though Bacillus sp. was not grown on alkaline conditions (>pH 8.0). In addition, the activity of xylanase was over 60% at pH 10.0. At the ambient temperature, the enzyme was stable over a pH range of 5.0 to 9.0 for 10 h, indicating that the enzyme is thermostable and alkalotolerant. The activity of xylanase was completely inhibited by metal ions including Hg$^{2+}$ and Fe$^{2+}$, while EDTA, phenylmethylsulfonyl fluoride (PMSF), $\beta$-mercaptoethanol and SDS didn't affect its activity. The enzyme was also identified to exert no activity on carboxymethylcellulose, laminarin, galactomannan, and soluble starch.

• Asian-Australasian Journal of Animal Sciences
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• 제3권2호
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• pp.115-120
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• 1990

Extracellular nuclease(s) in buffalo rumen fluid were purified from strained rumen fluid by a procedure involving Seitz filtration, acetone fractionation and gel filtration on Sephadex G-100. The enzyme resolved into two peaks exhibiting both DNase and RNase activities. The molecular weight of enzyme corresponding to peaks I and II were approximately 30,000 and 12,000 respectively. The properties of enzymes from the two peaks, however, were same. Optimum temperature for both DNase and RNase activities was at $50^{\circ}C$. Whereas DNase activity was stable upto $60^{\circ}C$, RNase activity was stable only up to $50^{\circ}C$. DNase activity recorded two pH optima, one at pH 5.5 and the other at pH 7.0. RNase activity recorded a broad pH optimum between pH 6.0-8.0. pH stability of the enzyme coincided with pH optima for both the activities. DNase activity was stimulated by $Mg^{2+}$ and $Mn^{2+}$ and inhibited by $Fe^{2+}$, $Zn^{2+}$, $Hg^{2+}$ and $Ag^+$. RNase activity was also stimulated by $Mg^{2+}$ and $Mn^{2+}$ and inhibited by $Cu^{2+}$, $Fe^{2+}$, $Zn^{2+}$, $Hg^{2+}$ and $Ag^+$. Reducing agents stimulated both the activities.