• 미생물학회지
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• 제29권3호
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• pp.167-171
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• 1991

An intracellular protease from cells of Pseudomonas carboxydohydrogena grown on nutrient broth was purified to better than 95% homogeneity in five steps using azocaseine as a substrate. The molecular weight of the native enzyme was determined to be 125, 000. Sodium dodecyl sulfate-gel electrophoresis revealedat least two non-identical subunits of molecular weight 70, 000 and 56, 000. The enzyme activity was completely ingibited by phenylmethylsulfonyl fluoride and diisopropyl fluorophosphate. The enzyme was also inhibited by $Mg^{2+}$ , $Zn^{2+}$ , $Cd^{2+}$, $Cu^{2+}$ , and $Fe^{2+}$ , but was stimulated by iodoacetamide. Maximal reaction rate of the enzyme was observed at pH8.0 and 30.deg.C. The isoelectric point of the enzyme was found to be 7.5. The enzyme was unable to hydrolyze carbon monoxide dehydrogenase.

• 한국식품영양학회지
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• 제7권1호
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• pp.1-7
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• 1994

To investigate the characteristics of active sites of the D-xylanase and $\beta$-xylosidase purified from Penicillium verruculosum, effects of various chemicals on the enzyme activity were analyzed. The D-xylanase was activated by Cua), however it was inhibited by metal ions, Hg2+ and Mna+, by chemicals, N-bromosuccinimide, iodine, diethylpyrocarbonate, and 2,3-butanedione. These results suggested that the D-xylanase from Penicillium verruculosum contained tyrosine, histidine, arginine and tryptophan at the active center. The $\beta$-xylosidase was inhibited by Hg2+, N-bromosuccinimide and sodium dodecyl sulfate, however it was not effected by Mn2+ and Cu2). It was suggested that the enzyme contained tryptophan at the active center.

• 한국식품영양과학회지
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• 제6권1호
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• pp.27-33
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• 1977

The alkaline protease was isolated from the culture of Penicillium species (P-46) grown in the wheat bran media. The crude purification of this enzyme was carried out by extraction with distilled water and precipitated with 0.7-saturated ammonium sulfate, then dialysis for 3days. The activity of this enzyme was determined by Folin's colorimetric method. The results were as follows; 1. The optimum pH and temperature of this enzyme were pH 8.4 and $45^{\circ}C$. 2. This enzyme was stable at pH $7.0{\sim}9.0$. 3. This enzyme was not inactivated by treatment in lower temperature than $30^{\circ}C$. 4. The activity of this enzyme was strongly inhibited by $Hg^{++}$ and $Cu^{++}$, but slightly by $Ag^+$ 5. This enzyme was not inhibited by cystein, thiourea, ${\varepsilon}-aminocaproic$ acid, 2, 4-DNP, EDTA but strongly inhibited by PCMB.

• 통합자연과학논문집
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• 제7권2호
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• pp.120-123
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• 2014

When a hydrophobic and hydrophilic environments of bis(2,2'-bipyridyl) copper(II) ($Cu(bpy)_2{^{2+}}$) are produced in the presence of anionic surfactant sodium dodecyl sulfate (SDS), cyclic voltammetry is used to investigate the microscopic environments which occurs at the glassy carbon electrode. In order to see the relation between ${\Delta}E_p$ and a critical micelle concentration (CMC), ${\Delta}E_p$ vs. -Log[SDS] for the redox couples are plotted. The concentration at the intersection of two lines is 2.57 mM SDS, and this concentration can be determined as the CMC (relative error: below 0.03%; 2.63 mM SDS by surface tensiometry).

• 미생물학회지
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• 제19권1호
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• pp.31-37
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• 1981

Avicelase, CMCase and salicinase of A.phoenicis K.U. 175 were purified from wheat bran culture by salting out with ammonium sulfate, dialysis and successive column chromatography Sephadex G-100. Optimum pH and temperature of avicelase were pH 3.8-4.8, $35-55^{\circ}C$ and that of CMCase, salicinase were pH4.5-5.5, $45-60^{\circ}C$ and pH 4.5-6.0, $45-60^{\circ}C$ respectively. These enzymes were relatively thermostable, alkali unstable and inhibited by $Ca^{++},\;Mn^{++},\;Cu^{++},\;and\;Hg^{++}$. Km values of avicelase, CMCase and salicinase were calculated to be $1.5{\times}10^{-4}M,\;5.5{\times}10^{-4}M\;and\;2.75{\times}10^{-5}M$ and Vmax values $1.66{\times}10^{-4}mM/min,\;3.33{\times}10^{-4}mM/min\;and\;1.14{\times}10^{-4}mM/min$, respectively.

• Journal of Microbiology and Biotechnology
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• 제7권6호
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• pp.386-390
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• 1997

A xylanase from the Bacillus sp. strain DSNC 101, isolated from soil, was purified to homogeneity by anion-exchange and hydrophobic interaction chromatography followed by gel filtration chromatography. The enzyme cleaved xylan, but not carboxymethyl cellulose, Avicel, soluble starch, and pNPX. The main product of oat spelts xylan hydrolysates was xylobiose. The xylanase had a molecular weight of 25 kDa determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Optimum temperature and pH for the xylanase activity were $50^{\circ}C$ and 6.0, respectively. $K_{m}\;and\;V_{max}$ of the enzyme for oat spelts xylan were 12.5 mg of xylan/ml and 869.5 unit/mg of protein, respectively. Xylanase was completely inhibited by Hg, Cu, and N-bromosuccinimide, but was stimulated by Ca, Co, and Mg.

• 한국소성가공학회:학술대회논문집
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• 한국소성가공학회 2008년도 춘계학술대회 논문집
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• pp.482-484
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• 2008

Anodic aluminum oxide (AAO) which prepared with two-step anodizing method (with dissimilar solutions) was used as a template to fabricate highly ordered, free standing metal nano-rods. AAO nano-template technique can realize self-organized hexagonal pore structure with nanometer dimension size, it's easy to control pore diameter, length and density by varying anodizing conditions. Ni and Ni/Fe/Cu multi-metal layer nanorods were electrochemically deposited into AAO nano-template by AC voltage in simple sulfate solutions.. The properties of samples are tested by X-ray diffraction (XRD), field emission microscopy (FE-SEM).

• 대한약학회:학술대회논문집
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• 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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• pp.146.1-146.1
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• 2003

A major protein was isolated from ginseng root (Panax ginseng C.A. Meyer) using a combination of ammonium sulfate fractionation, gel filtration chromatography, ion-exchange FPLC. Electrophoretic and gel permeation chromatographic studies revealed that the major protein, GMP, is composed of two subunits of approximately 28 kDa. In this, investigated the ability of GMP to inhibit the oxidation of low-density lipoprotein (LDL). GMP inhibited $Cu^{2+}$ (5$\mu$M)-promoted oxidation of LDL (125$\mu$g protein/mL) in a dose-dependent mamer (0~5 $\mu$M), with a maximal inhibitor at GMP/copper ratio of 1:10 and an $IC_{50}$ value of 0.2 $\mu$M, as determined by measurement TBARS. (omitted)

• 자원환경지질
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• 제29권1호
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• pp.65-75
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• 1996

대구(大邱) 달성중석(達城重石) 폐광산(廢鑛山)에서 유출(流出)되는 유해(有害)한 산성광산(醒性鑛山) 폐수처리(廢水處理)를 위한 인공(人工) 소택지(沼澤池) 방법(方法)을 제시(提示)하였다. 황산염(黃酸鹽) 환원(環元) 박테리아 (SRB)를 이용(利用)한 약 2개월(個月)의 실내실험(室內實驗) 결과(結果) 폐수중(廢水中) 중금속(重金屬) 원소(元素) 제거효율(除去效率)은 Fe, Al, Cd, Cu와 Zn은 99-100%, Mn은 90%이며 pH는 5.12에서 7.60으로 상승(上昇)되었다. 황산염(黃醒鹽) 환원(還元) 박테리아의 먹이인 기질(基質)들 (Substrates)과 달성광산(連城鑛山) 폐수(廢水)의 실험(實驗)에서는 버섯퇴비(堆肥)가 참나무 퇴비(堆肥)보다 11배(倍) 정도(程度) SRB의 영향분(營養分)인 Lactate가 유출(抽出)됨이 밝혀졌다. 황산염(黃酸鹽) 환원(還元) 박테리아 소택지(沼澤池)의 내용물(內容物) 구성(構成)은 다음과 같다; 1) 최하부(最下部)에 25cm 높이의 고품질(高品質) 석회석(石灰石)(직경(直徑) 5cm)을 채운다 : 2) 70% 참나무 퇴비(堆肥)와 30% 버섯 퇴비(堆肥)의 혼합퇴비(混合堆肥)와 황산염(黃酸鹽) 환원(還元) 박테리아 입자(粒子)들을 잘 섞어서 25cm 높이로 석회암층(石灰岩層)위에 둔다 : 3) 혼합퇴비(混合堆肥)에 의한 석회암(石灰岩) 사이의 간극축소(間隙縮小)를 막기 위하여 석회암층(石灰岩層)과 혼합퇴비(混合堆肥) 중간(中間)에 Geotextile을 깔아둔다. 실제(實際) 현장적용(現場適用)을 위(爲)한 소택지(沼澤池) 크기는 중금속(重金屬) 부하량(負荷量)과 투수율(透水率) 에 따라서 계산(計算)한 결과(結果)-1편(片)은 $15m{\times}15m{\times}1m$, -2편(片)은 $5.3m{\times}5.5m{\times}1m$, 그리고 -3편(片) 하부(下部)에 $52m{\times}52m{\times}1m$임이 밝혀졌다. 그러나, -3편(片)의 경우는 소택지(沼澤池)가 너무 크므로 동일(同一) 소택지(沼澤池) 5~15개(個)의 작은 cell들로 분리함이 좋다.

• 한국미생물·생명공학회지
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• 제31권3호
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• pp.224-229
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• 2003

경기도 일대의 가금류 공장부근 토양로부터 keratinolytic protease 생산성이 우수한 균주 KP-364를 선별하여 본 효소를 정제하고 일반적인 특성을 조사하였다. 본 효소는 ulkafiltration, ammonium sulfate fiactionation, DEAE-cellulose ion-exchange chromatography, Sephadex G-150 gel filtration 등을 통하여 정제되었으며 회수율은 25.2%이었다 SDS-PAGE와 gel filtration으로. 단일성과 분자량을 추정한 결과 전기영동 상에 단일 band를 나타내었으며 분자량은 약 36,000 dalton이였으며 1개의 subunit로_구성되어 있었다. 효소반응의 최적조건을 검토한 결과 최적 pH는 6.5, pH 3.0에서 10.0까지 90%이상의 활성을 나타냈으며 반응 최적 온도는 $37^{\circ}C$이였고 $60^{\circ}C$에서 1시간동안 80%이상의 활성을 유지하였다. 정제된 효소의 활성은$ FeSo_4$, KCI, $Li_2$$SO_4$를 첨가하였을 때 증가하였으며 $Ag_2$$SO_4$, $CuCl_2$, $HgCl_2$에 의해 저해되었다. 또한 EDTA, EGTA에 의해 저해되는 것으로 보아 metalloprotease의 일종이라고 판단되며 $Li^{ +}$를 cofactor로 함유하고 있는 것으로 조사되었다.