組織素 分解酵素를 生成하는 高溫性 곰팡이의 分離 및 特性

성낙계,강인수,박채규,정영철,김두현 慶尙大學校 1990 論文集 Vol.29 No.1

고온에서 잘 생육하고 cellulose 및 xylan 분해력 이 우수한 곰팡이를 분리할 목적으로 pH5.0, 50℃, Czapek-Dox pulp 배지에서 celluase complex와 xylanase생산이 우수한 곰팡이 H-702균주를 최종선정하여 균학적 성상을 조사한 결과, Aspergillus속과 거의 일치하였으며, 본 공시균주가 효소 생산에 미치는 영향과 효소학적 성질의 결과를 요약하면 다음과 같다. 생육 및 효소생성의 최적온도는 50℃이고, 균체증식 최적 pH는 5.0, cellulase 생산 최적 pH 는 4.5 xyanases는 4.0으로 나타났으며, 효소최대 생성 배양 4일째에, 균체증식은 약 3일경에 최대에 도달하였다.또한 α-1, 4-linkage를 가진 섬유성 물질 왕성하였으며 glucose 와 같은 저분자물질에서는 효소생합성이 현저히 저해되었는데 이런 결과로 볼때 이균주는 carbon catabolite repression을 받고 있었다. 효소생산에 적합한 탄소원으로는 α-cellulose,avicel, filter paper 등 이였으며, 질소원으로는 암모니아가 효과적이었으며 무기염류는 Ca??, Mg??, Mn??, Co??에서 효소생합성이 좋은것으로 나타났다. 계면활성제는 0.15% Tween 80이 좋았다. 개선된 KD배지에서는 각종 효소활성도가 1.2-1.6배 증가하였으며 또한 KD배지에서 각종탄소원을 지질로하여 효소 생합성을 조사한 결과 3% a-cellulose 에서 효소활성도가 좋았고 값싼 기질인폐신문지에서도 효소활성이 높게 나타났다. 조효소의 최적 온도는 cellulas complex 는 70℃, xylanase는 60℃로 나타났으며 열안정성은 cellulas complex 70℃까지는 30분간 , 80℃에서는 잔존활성이 약 93%였고 xylanase는 70℃에서도 거의 안정하였다.최적 pH는 cellulas complex는 5.0, xylanase는 5.5였으며, pH안정성은 3.0-8.0까지 안정하였다.조효소의 미치는 금속이온의 영향은 Ca??,Mg?? Mn??에의해 활성화 되었으며 Pb??, Cu??, Mg?? 에 의해 현저히 저해 현상을 나타냈다. In order to isolate a fungus which grow well in the high temperature and has the excellent decomposing power of cellulose and xylose a fungus. H-702 which produced potently cellulase complex(CMCase,avicelase and β-glucosidase) and xylanase in Czapek-Dox pulp medium (pH 5.0, 50℃) was finally selected. Then as a result of its bacteriological properties investigated it was almost the same properties as Apergillus sp.. The effect influencing to the enzyme production of the isolated strain and enzymological properties are followed. The optimal temperature and pH for cell growth and enzyme production were 50℃, 5.0, 4.5 and 4.0.respectively . The highest production of enzyme was shown when the culture time was three days and the greatest growth of cell was shown about after two days. In the cellulosic materials(CMC.avicel and α-cellulose etc.) containing α-1.4-linking the vigorous production if enzyme was shown and in the small molecular substance such as glucose was remarkably repressed. According to these results, this stain was under the control of carbon catabolite repression.α-cellulose , avicel and filter paper were suitable for carbon source in the enzyme production and NH? for nitrogen source and Ca??, Mg??, Mn?? and Co?? for inorganic salt. 0.15% Tween 80 was a good surface active agent. In improved KD medium each enzyme activity was increased 1.2 to 1.4 times. As a result of investigating enzyme biosynthesis, which each carbon source was used as substrate in the KD medium, it was shown a good enzyme activity. The optimal temperature of crude enzyme in cellulase complex and xylanase were 70 ℃and 60℃, respectively. Thermal stability was shown for 30 minutes until 70℃in cellulase complex and its residual activity at 80℃ was about 93%. It almost was stable at 70℃in xylanase. The optimal pH for cellulase complex and xylanase were 5.0 and 5.5.respectively and they were stable in the range of pH 3.0 TO 8.0. The crude enzyme was activated by Ca?? , Mg??and Mn?? but inhibited by Pb??, Cu?? and Ag?? remarkably.

Cellulase의 利用에 關한 硏究 : 第 1 報 大豆蛋白의 抽出에 對하여 Ⅰ. On the extraction of the soybean protein

金明燦,成洛癸,奇宇京 진주농과대학 1969 진주농과대학 연구논문집 Vol.- No.8

絲狀菌 Cellulase의 食品加工에의 利用의 一環으로 大豆와 비지에 對하여 Protein의 抽出試驗을 하였으며 實地 豆腐製造에 利用하여 다음과 같은 結果를 얻었다. 1) 本實驗室에서 製造한 Trichoderma 劑 酵素는 大豆와 비지에 對하여 Protein 抽出率이 높았다. 2) Trichoderma 酵素에 混在하는 大部分의 Protease는 熱處理(60℃30分)에 依하여 Cellulase component의 많은 失活없이 除去되었다. 3) 熱處理한 同 Trichoderma Cellulase를 使用하여 大豆와 비지로 부터 豆腐를 만들어 顯著한 收量 增加를 얻었다. As the part of the utilization of celluloytic enzyme derived from Trichoderma viride to the food processing, the extractability of the protein from soy bean and soy bean refuse was studied and some practical point in the preparoion of the soy bean curd was investigated. The results obtained were summerized as follows: 1) The crude enzyme from Tricoderma viride prepared in our laboratory had high extractability of protein from both soy bean and soy bean refuse. 2) Most of protease from Trichoderma viride was eliminated with little loss of celluloytic activity by heat treatment. 3) The increased yield of soy bean curd from soy bean refuse or soy bean was obtained using heat treated crude enzyme.

노인성질환 환자의 돌봄을 위한 전반적인 상태 평가표 및 돌봄을 이한 육체적 노동 요구 평가표의 타당도 및 신뢰도

김태유,김상윤,임병훈,권오영,최낙천 대한노인병학회 2002 대한노인병학회지 Vol.6 No.4

살충성 O,O-Dimethyl-O-(3-Methyl-4-Nitrophenyl)-Phosphorothioate (Sumithion^�)의 전기화학적 환원반응에 미치는 Micell의 영향

成洛道,明平根,朴勝熙,金日光 圓光大學校 基礎自然科學硏究所 1987 基礎科學硏究誌 Vol.6 No.3

The electrochemical reduction of sumithion in various surfactants, NaLS, CTABr, Trition X-100 and in acetonitrile solution has been examined by DC, DP polarography and cyclic voltammetry(CV). Especially, in anionic surfactant, NaLS solution, the height of reduction wave is dramatic eliminated and half-vale potentials are shifted to strong negative potential (-2.7 volt vs. Ag-AgCl) by repulsion of nitro group in sumithion and anionic micell surfaces. the processes of reduction of sumithion were irreversibly electrochemical mechanism and the result of the reaction at high cathodic potential (-2.7 volt vs. Ag-Agl) by repulsion of nitro group in sumithion and anionic micell surfaces. The processes of reduction of sumithion were irreversibly electrochemical mechanism and the result of the reaction at high cathodic potential (-2.7 volt vs. Ag-AgC1), O,O-dimethy1-O-(3-methylhydoxyaminophenyl) phosphorothioate is formed as major product via O,O-dimethyl-O-(3-methylhydoxyaminophenyl) phosphorothioate in NaLS micell solution.

살충성 O,O-Dimethyl-O-(3-Methyl-4-Nitrophenyl)-phosphorothioate (Sumithion^�)의 전기화학적 환원반응에 미치는 Micell의 영향

成洛道,明平根,朴勝熙,金日光 충남대학교 약학대학 의약품개발연구소 1986 藥學論文集 Vol.2 No.-

The electrochemical reduction of sumithion in various surfactants, LaLS, CTABr, Triton X-100 and in acetonitrile solution has been examined by DC, DP polarography and cyclic voltammetry (CV). Especially, in anionic surfactant, NaLS solution, the height of reduction wave is dramatic eliminated and half-wave potentials are shifted to strong negative potential (-2.7 volt vs. Ag-AgCl) by repulsion of nitro group in sumithion and anionic micell surfaces. The processes of reduction of sumithion were irreversibly electrochemical mechanism and the result of the reaction at high cathodic potential (-2.7 v. vs. Ag-AgCl), O,O-dimethyl-O-(3-methylhydoxyaminophenyl) phosphorothioate is formed as major product via O,O-dimethyl-O-(3-methylnitrosophenyl) phosphorothioate in NaLS micell solution.

살충성 O,O-Dimethyl-O-(3-Metyl-4-Nitrophenyl)-phosphorothioate (Sumithion^�)의 전기화학적 환원반응에 미치는 Micell의 영향

成洛道,明平根,朴勝熙,金日光 圓光大學校 基礎自然科學硏究所 1988 基礎科學硏究誌 Vol.7 No.3

The electrochemical reduction of sumithion in various surfactants, NaLS, CTABr, Triton X-100 and in acetonitrile solution has been examined by DC, DP polarography and cyclic voltammetry (CV). Especially, in anionic surfactant, NaLS solution, the height of reduction wave is dramatic eliminated and half-wave potentials are shifted to strong negative potential (-2.7 volt vs. Ag-AgCl) by repulsion of nitro group in sumithion and anionic micell surfaces. The processes of reduction of sumithion were irreversibly electrochemical mechanism and the result of the reaction at high cathodic potential (-2.7v. vs. Ag-AgCl), O,O-dimethyl-O-(3-methylhydoxyaminophenyl) phosphorothioate is formed as major product via O,O-dimethyl-O-(3-methylnitrosophenyl) phospho-rothioate in NaLS micell solution.

N-(benzoyl)-C-(N-methylanilino)imidoylchloride 유도체의 가수분해 반응메카니즘

權奇星,李龍九,成洛道,金千石 충남대학교 기초과학연구소 1993 연구논문집 Vol.13 No.-

25℃의 50%(v/v) 메탄올-물의 혼합용매 속에서 pH 변화에 따른 X-치환된 N-(benzoyl)-C-(N-methylanilino)imidoylchloride(s)들의 가수분해 반응속도상수를 측정하여 반응속도식, 치환기효과, 용매효과, 염효과, 열역학적 활성화 파라미터 및 가수분해반응 생성물 분석 등의 결과로부터 pH3.0∼10.0까지의 사이에서는 azocarbonium ion 중간체를 지나는 S_N1형 반응, pH3.0 이하와 pH10.0 이상의 pH에서는 사면체 중간체를 지나는 친핵성 첨가-제거반응(Ad_N-E)이 일어남을 제안하였다. Rate constants of hydrolysis of N-(benzoyl)-C-(N-methyl-anilino)imidylchlorides were determined by UV spectrophotometry in 50% (v/v) aqueous methanol at 25℃. On the basis of rate equation, substituent effect, solvent effect, salt effect, thermodynamic parameters and hydrolysis product analysis, it may be concluded that the hydrolysis of N-(benzoyl)-C-(N-methyl-anilino)imidylchlorides proceed through S_N1 mechanism via azocarbonium ion intermediate in the range of from pH 3.0 to pH 10.0, while above pH 10.0 and below pH 3.0 the hydrolysis proceeds through nucleophilic addition-elimin ation (Ad_N-E) mechanism.

p-Methoxystyrylphenylsulfone의 가수분해 반응메카니즘에 대한 반응속도론적 연구

權奇星,高東成,朴文奎,金演斗,成洛道 충남대학교 기초과학연구소 1981 연구논문집 Vol.2 No.-

The rate constants for the hydrolysis of p-methoxystyrylphenylsulfone were determined at wide pH ranges by means of UV spectrophotometer and the rate equations which could be applied to the experimental results were obtained. Form the facts, reaction mechanism was proposed : above pH 11.5, the rate is only dependent on the concentration of hydroxide ion and below pH 9.5, the reaction is initiated by the attack of a water molecule on the activated carbon-carbon double bond. In the range of pH from 9.5 to 11.5, these two reactions occur competitively.

Phenyl-N-benzoylchlorothioformimidate 誘導體의 加水分解 反應 메카니즘

權奇星,金千石,李龍九,成洛道 충남대학교 기초과학연구소 1992 연구논문집 Vol.12 No.-

25℃의 30%(v/v) dioxane-물의 혼합용매 속에서 pH 변화에 따른 X와 Y-치환된 phenyl-N-benzoylchlorothioformimidates(S)들의 가수분해 반응 속도상수를 측정하여 반응속도식을 유도하고, 경계 궤도 함수 상호작용, 용매효과, 일반 염기 촉매효과, 열 역학적 활성화 파라미터, 및 가수분해반응 생성물 분석 등의 결과로부터 pH 10.0 이하의 낮은 pH에서는 azocarbocation 중간체를 지나는 S_N1형 반응, pH 11.0 이상의 높은 pH에서는 사면체 중간체를 지나는 친핵성 첨가-제거(Ad_N-E)반응 그리고 pH 10.0과 11.0 사이에서는 이들 두가지 유형의 궤도 조절 반응이 서로 경쟁적으로 일어남을 제안하였다. The rate constants of hydrolysis of phenyl-N-benzoylchlorothioformimidates were determined by UV. spectrophotometry in 30% (v/v) aqueous dioxane at 25℃. On the basis of rate equation, general base catalysis, solvent effect, substituent effect, thermodynamic parameters, frontier orbital interaction and hydrolysis product analysis, it may be concluded that the hydrolysis of phenyl-N-benzoylchlorothioformimidates proceed through S_N1 mechanism via azocarbocation intermidiate below pH 10.0, while above pH 10.00 the hydrolysis proceeds through nucleophilic addition-elimination (Ad_N-E) mechanism. In the range of pH from 10.0 to 11.0 these two reaction occur competitavely.

Pectolytic Enzyme에 關한 硏究 (第一報) : 分離細菌 ??가 生産하는 Macerating Enzyme와 Pectolytic Enzymes에 關하여 Ⅰ. Macerating Enzyme and Pectolytic Enzymes Produced by Isolated Bacteria (??)

李千洙,金鍾奎,奇宇京,成洛癸 慶尙大學校 1972 論文集 Vol.11 No.-

고구마 軟腐病所에서 分離한 細菌 ??가 生産하는 酵素中에서 macerating acton을 하는 酵素를 究明하기 위한 資料로 쓰기 위해 macerating enzyme의 生成에 미치는 pectin의 影響과 生成한 macerating enzyme와 pectolytic enzymes의 一般전 性質을 조사한 결과는 다음과 같다. 1. 細菌 ??는 酵素生成培地(wheat bran media)에 pectin을 加하므로써 macerating enzyme을 效果的으로 生産했다. 2. pectic acid liquefying activity, pectin liquefying activity, pectin esterase,와 macerating enzyme은 各各 1) 最適作用 pH가 7.2∼7.8, 7.2, 6.0, 6.5∼7.5 2) 最適作用溫度는 50℃, 50℃, 60℃, 50℃ 3) pH 安定性은 3.0∼8.0, 5.0∼8.0, 3.0∼8.0, 및 3.0∼8.0이었다. The influence of pectin on production of macerating enzyme by isolated bacterial ?? and the enzymological properties of its macerating enzyme produced and pectolytic enzymes were studed. The results obtained were summarized as follows: 1. Macerating enzyme was effectively produced in the media adding pectin. 2. The optimum pH of pectic acid liquefying activity, pectin liquefying activity, pectin esterase and macerating enzyme were 7.2∼7.8, 7.2, 6.0 and 6.5∼7.5 respectively. 3. The optimum temperature of pectic acid liquefying activity, pectin liquefying activity and macerating enzyme were 50℃., and that of pectin esterase was 60℃. 4. The pH stability of pectic acid liquefying activity, pectin esterase and macerating enzyme were 3.0∼8.0, and that of pectin liquefying activity was 5.0∼8.0.