• 한국환경과학회지
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• 제11권10호
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• pp.1103-1108
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• 2002

In order to evaluate the degradation organophosphorus pesticide, EPN, in water environment, the effects of water temp.(10$^{circ}C,\;30^{\circ}C$), pH(3-11) and sunlight on its degradation were investigated during 10 days. The degradation rate of EPN(200 rpm) was faster at higher water temp. and higher pH, i.e., its degradation rate at pH 3, 5, 7, 9, 11 was 57, 63, 66, 69, 75%(1$0^{\circ}C$), and 70, 74, 79, 91, 97%(3$0^{\circ}C$) after 10 days, respectively. The effect of water temp. on its degradation was little in acidic condition, but was rather great in alkaline condition, with time. EPN was degraded fast at the alkaline condition by photolysis. At the condition of pH 11, EPN was degraded fast at the early stage in the first 2 days, but after that the degradation rate was weakened.

• 콘크리트학회논문집
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• 제29권1호
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• pp.85-92
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• 2017

본 연구에서는 붕소화합물을 혼입하여 제작한 모르타르의 특성에 대한 검토를 수행하였다. 사용된 붕소화합물은 pH 값에 따라 산성 및 약알칼리성, 강알칼리성으로 구분하여 선별한 것으로 산성 기반인 붕산(AA)과 약알칼리 기반의 붕사(AB), 강알칼리성인 붕사(HB)이다. 실험은 모르타르의 물리적 화학적 특성을 파악할 수 있는 pH 측정 및 응결 시험, 압축강도 시험을 수행하였으며 모르타르 내 미세구조 분석을 위해 SEM 촬영을 수행하였다. pH 측정 결과 붕소화합물을 혼입한 시험체 전반적으로 기본 모르타르보다 pH가 낮게 측정되었으며 시간이 지남에 따라 pH가 저하되는 양상을 보였다. 또한, 응결 시험에서도 기본 시험체보다 초결 및 종결 시점이 늦게 발생되었으며 알칼리도에 따라 응결 지연을 저감할 수 있다는 기존 문헌과 다소 다른 결과를 나타냈다. 압축 강도 및 SEM 촬영 결과, 붕소화합물의 종류 및 성분에 따라 강도 등의 물리적 성능이 결정되기 때문에 이를 고려하여 최적 혼입량을 결정하는 것이 바람직할 것으로 판단된다.

• 미생물학회지
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• 제34권3호
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• pp.82-86
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• 1998

Yarrowia lipolytica 504D가 생산하는 alkaline proteinase를 정제한 결과, 분자량은 32,000으로 나타났고, pH 9.5와 $42^{\circ}C$에서 최적활성을 보였으며, pH 4-10의 범위와 $45^{\circ}C$까지 비교적 안정한 것으로 나타났다. PMSF를 비롯하여 EDTA, EGTA, phenanthrolin도 효소활성을 저해하여 정제효소가 serine proteinase인지 metal proteinase인지 불확실하였다. 그러나 28% 활성증가를 보인 $Cu^{2+}$ 외에 $Zn^{2+}$를 비롯한 대부분의 무기염들이 효소활성을 증가시키지 못하였고, 또한 EDTA의 첨가로 불활성화된 효소도 Ca 염의 첨가로 활성이 복원되었다. 따라서 정제효소는 serine proteinase(E.C. 3.4.21.14)로 추정되었다.

• 마이크로전자및패키징학회지
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• 제18권4호
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• pp.43-48
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• 2011

탄소 기지상에 니켈도금을 하여 다공성 MCFC의 전극으로 사용하기 위하여 탄소 기지위에 산성용액과 염기성용액을 이용하여 무전해 니켈도금을 하였다. 알칼리 용액에서의 도금속도가 산성용액에서의 도금속도보다 빨랐으며 두가지 용액에서 pH가 증가함에 따라 도금속도가 증가하였다. 산성용액에서의 잔류응력은 압축응력을 보였으며 알칼리용액에서는 높은 인장응력을 보였으며 높은 잔류응력으로 인하여 pH 11 이상에서는 표면균열이 발생하였다. Thiourea를 첨가하였을 경우 0.5 ppm까지의 저농도에서 도금속도가 증가하다가 이후 감소하였으며 1.5 ppm 이상에서 두가지 용액에서 모두 도금이 더 이상 진행되지 않았다. Succine 산을 첨가한 경우 5 g/L까지 속도가 증가하다가 감소하여 일정한 값을 유지하였다.

• 한국미생물·생명공학회지
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• 제22권1호
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• pp.59-64
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• 1994

The production and the characteristics of protease produced by Bacillus sp. SH-8 and Bacillus sp. SH-8M were investigated under the different pH conditions. Bacillus sp. SH-8 and Bacillus sp. SH-8M showed the maximum activity of protease at 60 hours(70 units/ml) AND 96 houre(50 units/ml) cultivation, respectively, under the alkaline condition(pH 10.2). However, Bacillus sp. SH-8M exhibited the maximum activities in 8 days cultivation at pH 6.9 and in 6 days cultivation at pH 7.7 Bacillus sp. SH-8M showed the protease activity at the pH change from alkaline to neutral condition, whereas Bacillus sp. SH-8 did not. In addition. all the enzymatic characteristics of protease produced by Bacillus sp. SH-8 and Bacillus sp. SH-8M were similar with the regardless of different pH conditions.

• 한국미생물·생명공학회지
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• 제22권5호
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• pp.515-521
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• 1994

A bacterial strain, which showed the high protease activity at low temperature and the high tolerance for the surfactant, was isolated from soil and identified as Xanthomonas sp. YL-37. The optimal temperature, initial pH, and cultivation time for the production of the alkaline protease by Xanthomonas sp. YL-37 were 20$\circC , 11.0, and 84 hours, respectively. In the jar fermenter culture of Xanthomonas sp. YL-37, the alkaline protease activity was about 15,000 DU/ml/-broth after cultivating for 108 hours. The optimal pH and temperature for the protease activity were 70$\circC and 11.0, respectively. The protease was relatively stable at the pH range of 7.0~12.0 and at the temperatures below 50$\circC . The protease activity at 20$\circC was about the level of 40% of its activity at 70$\circC . The enzyme was suggested as a serine protease because the enzyme activity was inhibited by phenylmethane sulfonyl fluoride, a serine modifier.

• 한국수산과학회지
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• 제23권5호
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• pp.401-406
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• 1990

In order to assess fish meal as food protein source which contains heat denatured pro-tein, functional properties of fish meal protein to be treated with alkaline were examined. Ratio of fish meal to 0.2N NaOH solution for extract solvent which were 1:10 showed good results of extracted and recovered amount of fish meal protein. pH 4.5, solubility of protein treated with alkaline revealed the lowest value. Until concentrations of alkaline treated protein solution reached $0.7\%$, its emulsifying capacity steeply decreased. Emusifying capacity of alkali treated protein were higher value at pH 9.0 than pH 4.0 and 7.0, and also were higher quantity in 0.5M NaCl solution than that of 0.1M. Heating time of fish meal protein to be treated with alkaline reached until 30 mins, its fat binding capacity indicated little change and that of heating time 60 mins decreased. Gel forming concentrations of fish meal protein to be treated with alkali for 15 mins or less were $20\%$ but those of 30 and 60 mins were $25\%$. When treating time of fish meal protein with alkali solution reached till 20 mins, viscosity of alkali treated protein solution steeply decreased.

• 한국수산과학회지
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• 제16권2호
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• pp.147-153
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• 1983

To check the differences of the digestive enzymes by the bait habits and the proteolytic activities of the fissile extracts from the fish, omnivorous filefish (Navodon modestus), carnivorous cat shark (Scilliorhinus tarazame) and bloodsucking hag fish (Eptatretus burgeri) were sampled for this experiment. The activity of crude alkaline protease extracted from the muscle and the internal organs of the samples was determined with casein as substrate. The activity of the proteolytic enzymes showed remarkable differences by the organs of the fish. The optimum condition of the pretenses from the muscle revealed in range of pH 7.8-8.3, at $60-65^{\circ}C$, while those of the enzymes from the internal organs were at about pH 8.2, $45-55^{\circ}C$, but those of hag fish were at about pH 6.7, $45-55^{\circ}C$. The proteolytic activity of the enzyme of alimentary canal in filefish and in hag fish was 57 and 11 times stronger than that of muscle, respectively. The crude enzyme from the alimentary canal of file fish showed the strongest proteolytic activity in samples submitted and that of cat shark was the lowest. The activity of pancreatic alkaline protease in cat shark was 50 fold higher than that of muscle alkaline protease in the fish.

• Mycobiology
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• 제32권2호
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• pp.74-78
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• 2004

An alkaline protease produced by Aspergillus niger C-15 was purified and characterized. The enzyme was purified 19.41-fold with a specific activity of 74150 U/mg and a recovery of 34.4% by gel filtration and ion exchange chromatography. The molecular weight of the enzyme was estimated to be 34 kDa. The optimum pH and temperature for the protease activity were pH 8.0 and $60^{\circ}C$, respectively. The enzyme activity inhibited by EDTA suggests that the preparation contains a metalloprotease. The enzyme activity of the metalloprotease was completely inhibited by 5 mM $HgCl_2$ and $FeCl_3$, while partially inhibited by $CuSO_4$, and $MnCl_2$. When polyols such as glycerol, mannitol, sorbitol and xylitol, were added to the reaction medium, most polyols tested enhanced protease activity. Especially, glycerol showed the highest effect. The alkaline metalloprotease was stable at high temperature and retained more than 90% of the initial activity at $60^{\circ}C$ and 86.4% under addition of glycerol.

• 펄프종이기술
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• 제29권3호
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• pp.87-94
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• 1997

As the paper market becomes more and more competitive, more mills will want to switch to alkaline papermaking to take advantage of the Vowing demand. Many papermakers have tried to do this without success in the past much like the American papermakers did in the late 1970's. The Problem is that runnability Problems occur, drainage slows, Presses pick drying becomes more difficult and sheet quality suffers as a result Sheet holes and breaks occur, and runnability becomes a real operating problem. Converting to alkaline papermaking is not as simple as turning off the alum. We must be aware of the numerous factions that alum served at acid pH and provide alkaline alternatives. It is the purpose of this paper to discuss methods of deposit control via charge neutralization and system control at alkaline pH. This article explains the concept as well as the measurement and control. The resultant benefits are seen in runnability, quality and profitability for the papermaker.