• 한국미생물·생명공학회지
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• 제10권3호
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• pp.197-203
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• 1982

The protopectinase from the culture extract of a Verticillium sp. was purified about 1000 fold by ammonium sulfate fractionation, DEAE-Sephadex treatment and Sephadex G-75 column chromatography. The purified enzyme was homogeneous on electrophoresis and its molecular weight was estimated to be 38000 by Andrew's gel filtration, method. The enzyme was almost stable under the temperature of 4$0^{\circ}C$ and within the pH range of 3-5. Its optimum pH and temperature were 4 and 4$0^{\circ}C$, respectively. The activity was markedly inhibited by galacturonic acid. The purified enzyme was able to macerate various kinds of plant tissues, such as radish, cucumber, onion, carrot, and potato. It also reduced the viscosity of pectin solution more rapidly than that of pectic acid solution and showed no lyase or CMCase activity.

• Applied Biological Chemistry
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• 제7권
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• pp.67-77
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• 1966

For the production of proteolytic enzyme wilth Aspergillus, the examination is made on the culture-time and koji extracting conditions, during producing koji. 1. The highest activity showed up when the culture-time took 50 hours for Aspergillus sojae and 60 hours for Aspergillus flavus. 2. When the cultured koji was extracted by a buffer solution and water, the former gave the product of higher activity until pH 7 through pH 12, and water until pH 3 through pH 7. 3. In the method of crushing and granule extractions, crushing extraction produced the one of higher activity than granule. 4. The highest activity showed up when Aspergillus sojae took 5 hours (Aspergillus flavus 4 hours) in the time of extracting enzyme solution. 5. The highest activity showed up when both Aspergillu sojae and Aspergillus flavus reacted and indicated $37.60^{\circ}C$ in the reaction temperature and activity.

• 한국농업기계학회:학술대회논문집
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• 한국농업기계학회 2005년도 하계 학술대회 논문집
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• pp.331-336
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• 2005

• 한국미생물·생명공학회지
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• 제25권1호
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• pp.51-55
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• 1997

To utilize the alkaline protease produced by Halomonas sp. ES-10 as an enzyme detergent, the crude enzyme was obtained by methanol precipitation and lyophilization. And it was processed to coated enzyme.The best mixing ratio of components such as coated enzyme, builders, actives, fillers and adjuvants on detergency was examined, and temperature and pH influencing detergency were also tested. Detergency test 0.15% detergent solution was carried out on EMPA test cloth #116 with shaking(90 rpm) for 10 min after 30 min of pretreatment. The detergent which contained coated-enzyme 1%, Zeolite 4A 20%, Tween 80 1. 5%, sodium borate 30%, sodium meta silicate 7.5% and water 40% showed about 90% of washing efficiency at 40$\circ $C and pH 10.0.

• Korean Chemical Engineering Research
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• 제53권1호
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• pp.6-10
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• 2015

효소 전극 anode와 PEMFC용 전극 cathode를 이용하여 효소연료전지를 구동하였다. 효소 anode는 그래파이트 분말과 효소로서 글루코스 산화제, 전자매개체로서 페로센을 혼합해 압축해서 만들고 Nafion 이오노머로 코팅하였다. anode 제조조건을 변화시키며 OCV를 측정해 효소 anode 제조 최적조건을 찾았다. 효소 anode 압축 시 최적 압력은 9.0 MPa였다. 효소 anode에서 그래파이트가 60%일 때 최고의 OCV를 나타냈다. anode 기질 용액의 최적 글루코스 농도는 1.7 mol/l이었으며, anode의 효소 활성은 7일 동안 안정적으로 유지되었다.

• 한국환경과학회지
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• 제8권1호
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• pp.19-26
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• 1999

The degree of pesticides accumulation in tap water in Taejon from June 1995 to Apr 1996 was measured by Ellman's coupled enzyme assay. Since organic phosphate and carbamate pesticides specifically inhibit the neurotransmitter modulating enzyme acetylcholinesterase(AChE), the enzyme activity can be used as a diagnosis for the pesticides accumulation in water and various samples. During the period of this study, the enzyme activity was changed almost every week. The lowest enzyme activity was 64 % of that of the control reaction and there are several days showing about 100 % enzyme activity. In general, the enzyme activity is higher in summer than other seasons especially early spring times. The pH value of tap water was very close to neutral(pH 7.0) and it seems that the enzyme activity was not affected by the small pH changes. Either boiling of tap water or addition of NaOH solution decomposed the pesticide components. These results show that AChE assay is a convenient, sensitive, and reliable method for detection of pesticides in water samples.

• 한국미생물·생명공학회지
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• 제19권4호
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• pp.377-382
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• 1991

우지를 lipase에 의해 지방산과 글리세린으로 분해하는 반응을 액상 및 고상에서 수행하였다. 올리브유를 기질고 lipase OF 360(일본 메이토사 제품)의 특성을 조사한 결과 최적 pH는 6, 최적 온도는 $37^{\circ}C$이었다. 우지를 기질로 액상 효소반응을 수행한 결과는 물사용량 80 wt/wt, 온도 $37^{\circ}C$, 효소사용량 200unit/g tallow 조건에서 93의 가수분해율을 얻을 수 있었다.

• 한국전기전자재료학회논문지
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• 제13권6호
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• pp.520-525
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• 2000

Glucose oxidase was immobilized in polypyrrole by electrosynthesis. The enzyme had an influence on the redox properties of a complex enzyme electrode. In the cyclic voltammograms of the enazyme electrode new peaks were appeared at the potential around 0.7V vs. Ag/AgCl in additional to the typical peaks for polypyrrole. The more immobilized the stronger the peaks became. During the cycling the pH of electrolyte solution was decreased to about 4.4 The reason for that is to be the proton released from the carboxyl in the glucose oxidase in order to keep on a charge neutrality of the oxidized enzyme. This fact suggests that the new peaks in the voltammograms are caused by the redox of glucose oxidase. In the AC impedance spectrum analysis of the electrode the diffusion of electrolyte anion was limited because of chained structure of the enzyme. The faradic impedance was large since the glucose oxidase is an insulator. Therefore when glucose oxidase is entrapped the enzyme should be limited in amount. Because the growth of the polypyrrole is accompanied both charge transfer and mass transport. For the traditional electrosynthesis that means amount of enzyme present in the electrode is limited to as much as film growable.

• Korean Chemical Engineering Research
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• 제54권2호
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• pp.171-174
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• 2016

효소 전극 cathode와 PEMFC용 전극 anode를 이용하여 효소연료전지를 구동하였다. 효소 cathode는 그래파이트 분말과 효소로서 Laccase, 산화환원 매개체로서 ABTS를 혼합해 압축해서 만들고 Nafion 이오노머로 코팅하였다. cathode 제조조건을 변화시키며 OCV를 측정해 효소 cathode 제조 최적조건을 찾았다. 효소 cathode 압축 시 최적 압력은 4.0 bar 였다. 효소 cathode에서 그래파이트가 95%일 때 최고의 OCV를 나타냈다. cathode기질 용액의 최적 글루코스 농도는 0.4 mol/l이었다.

• Journal of Chest Surgery
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• 제25권2호
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• pp.131-136
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• 1992

The effect of temperature of cardioplegic solution on myocardial preservation was studied using isolated rat heart perfusion technique. Twenty Sprague-Dawley rats, weighing 120~140gm, were pretreated with intraperitoneal injection of heparin sodium[300u/kg] and then the hearts were excised after cervical herniation 30 minutes later. The hearts were perfused in isolated working heart apparatus with oxygenated modified Tyrode solution at 37oC. After 10 minutes of non working heart perfusion, the hearts were subjected to arrest for 30 minutes by administration of 5cc cardioplegic solution at the temperature of 4oC [Group I ], 15oC [Group II], 25oC [Group III], 37oC[Group IV]. At the same time, the topical cooling of heart was performed using ice saline. After arrest, the hearts were reperfused by non working heart perfusion for 1 hour with modified Tyrode solution at 37oC. The CPK, GOT and LDH in reperfusate were measured at 5,20,40,60 minutes after start of reperfusion. With the values of those, we compared the effect of temperature of cardioplegic solution on myocardial preservation. The results were as follows; 1. The enzyme values in reperfusate were highest at 5 minute and after then declined. 2. At 5 minutes after reperfusion, the enzyme values in Group I were lower than those in other Groups. These results suggest that the cardioplegic solutions using for cardiac arrest and myocardial protection can be working better at 4oC than at any other temperature.