배양심근세포에 있어서 Glucose oxidase의 독성에 대한 천오두의 영향

이정헌(Jung Hun Lee),이강창(Kang Chang Lee),김상수(Sang Su Kim),홍기연(Gi Youn Hong),오연균(Yeon Kyun Oh),석승한(Seung Han Suk),이갑상(Gap Sang Lee),진복희(Bok Hee Jin),신홍철(Hong Chul Shin),류도곤(Do Gon Ryu),박승택(Seung Taeck Par 한의병리학회 2002 동의생리병리학회지 Vol.16 No.3

Bacillus subtilis YG-95가 생산하는 protease의 정제와 특성

변영각,김성호,주현규,이갑상,임무현,Byun, Young-Gag,Kim, Seong-Ho,Joo, Hyun-Kyu,Lee, Gap-Sang,Yim, Moo-Hyun 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.43 No.4

Bacillus subtillis YG-95가 생산하는 protease를 ammonium sulfate$(35{\sim}85%)$ precipitation, DEAE-separose 6B, sephadex G-100을 통해 분리, 정제하였고 정제된 효소의 특성을 조사하였다. SDS-PAGE로 확인된 효소의 분자량은 약 43 kilodalton이었다. 효소반응의 최적 pH 및 최적온도는 각각 약 pH 10.0와 $55^{\circ}C$이었으며, 효소는 $pH\;5{\sim}12$ 까지 넓은 pH범위에서 안정성을 보였고, $45^{\circ}C$까지의 온도에서 안정하였다. 본 효소는 $Fe^{3+}$와 $Al^{3+}$에 의해서 활성이 저해되었으며, 저해제 중에서는 O-Phenanthroline, PMSF, SDS에 의해서 80%이상 저해를 받았고 SPI에 대한 기질 친화도는 $K_m$은 1.28 mg/mL이었다. The protease produced by Bacillus subtilis YG-95 was purified by precipitating with ammonium sulfate, DEAE-sepharose 6B and Sephadex G-100 column chromatogtaphies and its purified enzymological characteritics were investigated. The molecular weight of purified protease was estimated about 43kilodalton by SDS PAGE The optimum pH and temperature for the purified protease activity were pH 10.0 and $55^{\circ}C$, respectively. The enzyme was stable in broad range of pH 5.0 to 12.0. and at the below $45^{\circ}C$. The purified enzyme activty was inhibited by $Fe^{3+}$ and $Al^{3+}$. The activity was significantly inhibited more than 80% by O-Phenanthroline, PMSF and SDS. The $K_m$ value of the purified enzyme against Soy Protein Isolate as a substrate was 1.28 mg/ml.

전통메주로부터 Protease 생산 균주의 분리, 동정 및 효소 생산조건

변영각,김성호,주현규,이갑상,임무현,Byun, Young-Gag,Kim, Seong-Ho,Joo, Hyun-Kyu,Lee, Gap-Sang,Yim, Moo-Hyun 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.43 No.4

A bacteria producing protease against soy protein was isolated from various traditional Me-Ju, in order to improve utililization and characteritics of soy protein hydrolysates reduced bitterness and advanced flavors. The optimal culture conditions for protease production was investigated. The isolated bacteria was identified as Bacillus subtilis by morphological and physiological charateristics and named Bacillus subtilis YG-95. The optimal culture condition of liquid medium for protease production by Bacillus subtilis YG-95 composed of 3.5% soluble starch, 3.0% soy protein isolate, 0.25%, dextrose, 0.5% NaCl, 0.25% $K_2HPO_4$ with on initial pH of 7.6, for 60 hrs at $45^{\circ}C$. 대두단백질 가수분해물의 이용과 특성 등을 향상시키기 위한 연구의 일환으로, 쓴맛성분이 적고 향미가 우수한 가수분해물의 제조에 이용되는 protease를 생산하기 위하여, 전국 각지역의 메주에서 대두 단백 분해 효소의 생산이 우수한 균을 분리하였고, 형태학적, 생화학적 특징을 검토한 결과, Bacillus subtilis로 동정 되었고, Bacillus subtilis YG-95로 명명하였다. 단백분해효소 생산을 위한 배지의 최적 조건을 검토한 결과 soluble starch 3.5%, soy protein isolate 3.0%, dextrose 0.25%, NaCl 0.5%, dipotassium phosphate 0.25%의 배지의 조건에서 배양 최적 pH는 7.6, 최적 배양온도는 $45^{\circ}C$, 최적 배양시간은 60시간으로 배양했을 때 효소의 생산에 최적조건이었다.

실차 운행정보를 이용한 온실가스 배출량 산정에 관한 연구

박건진(Park, Geon Jin),김필수(Kim, Pil Su),최상진(Choi, Sang Jin),한용희(Han, Yong Hee),이헌주(Lee, Heon Ju),이갑상(Lee, Gap Sang),장영기(Jang, Young Kee) 한국기후변화학회 2015 한국기후변화학회지 Vol.6 No.2

Ethylcrotonate에 對한 n-butylmercaptan의 親核性 添加反應 메카니즘과 그의 反應速度論的 硏究

成洛道,李甲湘 圓光大學校 1976 論文集 Vol.10 No.-

The rate constants for the addition reaction reaction of n-butylmercaptan to ethlyI crotonate have been measured by iiodometry and for the proposed reaction mechanism a rate equation whcih can be applied over wide pH range was obtained; ?? Below pH 6.5, the nucleophilic addition of n-butylmercaptan to ethylcrotonate is initiated by the attack of mercaptan molecule. Above pH 10.5, mercaptide ion is the only nucleophile to ethylcrotonate and in the range of pH from 6.5 to 10.5 these two reactions occur competitively.

아플라톡신에 대한 익모초의 돌연변이 억제 효과

안병용,이갑상,맹일경,송근섭,최동성 한국식품영양학회 1996 韓國食品營養學會誌 Vol.9 No.3

Escherichia coli PQ 37 균주를 이용한 SOS Chromotest계에서 아플라톡신 B_1의 돌연변이원성에 대한 생약재의 항돌연변이원성을 검색하였다. 익모초의 열탕 추출물은 Salmonella typhimurium TA 98 균주를 이용한 Ames 시험계에서 S9 혼합액의 첨가와 비첨가시 돌연변이원성을 나타내지 않았다. 그리고 익모초의 추출물은 아플라톡신 B_1으로 유도된 돌연변이원성에 대하여 항돌연변원성을 나타냈으나 익모초의 물추출물의 메탄올 수용부분(IMC-MS)은 아플라톡신 B_1으로 유도된 돌연변이원성에 대하여 용량반응의 항돌연변이 효과를 나타냈고, 물 수용분획에서는 comutagenic 효과를 나타내었다. IMC-MS와 아플라톡신 B_1을 혼합하여 일차 배양한 경우 아플라톡신 B_1으로 유도된 돌연변이원성에 대하여 가장 강한 억제 효과를 나타내었다. 또한 1차배양시 IMC-MS와 S9 혼합액을 첨가한 후 아플라톡신 B_1을 첨가하였을 때는 낮은 저해효과를 나타내었다. 일련의 배양 결과는 S9 효소의 불활성화에 의한 영향보다는 IMC-MS와 아플라톡신 B_1의 화학적 복합물을 형성하여 나타나는 저해 메카니즘일 가능성을 시사하고 있다. By the SOS chromotest which utilized Escherichia coli PQ 37, Korean medicinal plants had been screened to investigate the antimutagenic effect to aflatoxin B_1(AFB_1). Ikmocho(IMC, Leonurus sibiricus L.) was extracted with hot water. The extract was not found to be mutagenic in the Salmonella mutation test with or without metabolic activation, and the extract was showed to possess the antimutagenic properties towards AFB_1-induced mutation. The mutagenicity of AFB_1 was inhibited by methanol soluble fraction(IMC-MS) in dose-dependent. However, water-soluble fraction exhibited comutagenic activity. The greatest inhibitory effect of IMC-MS on AFB_1 mutagenicity occurred when IMC-MS was first incubasted, AFB_1 followed by a second incubation with the cells and S9 mixture. Also lower inhibition was occurred when S9 mixtures were first incubated, with IMC-MS followed by a second incubation with AFB_1. The results of the sequential incubation study support the probability that one mechanism of inhibition could involve the formation of chemical complex between IMC-MS and AFB_1 rather than deactivation of S9 enzyme.

전통메주로부터 대두단백질 가수분해효소 생산성 미생물의 분리 및 동정

김성호,임무현,주현규,이갑상,강민정 한국농화학회 2000 Applied Biological Chemistry (Appl Biol Chem) Vol.43 No.2

In order to develop the enzymatic hydrolysis system concerned with taste and flavor, strains having the high hydrolyzing activity on the soy protein were selected from some traditional Mejus. Two molds and one bacterium producing enzymes which were different in character of hydrolysis were isolated and identified. Leucine and azodye enzyme activities of both M4 and M5 were relatively high among in the isolated molds. And, leucine enzyme activity of B16 was the lowest in the isolated bacteria. These strains were isolated as microorganisms having a dissimilar hydrolysis pattern on the soy protein by enzymatic reactions. Mold M4 on the culture solid media was mycelium colors of white and its sclerotia colors were changed from white to black. According to the result of slide culture, radial conidial head, subclavate vesicle, conidia of subglobose, stipes of uncolored with smooth walls and metula and phialides were existed. Because M4 was taxonomically similar to the characteristics of Aspergillus oryzae (ahlburg) species, M4 was identified and named as Aspergillus oryzae M4.Mold M5 showed white and black mycelium on the MEA medium. Mold M5 colony exhibited grayish-green color and have long(7 ㎜) sporangiophores at slide culture. Sporangia became brownish-gray and the wall of larger sporangia was broken to form small collars, and smaller sporangia were fomed continually from large basal membrane. Columella is globose and hyaline, and sporangiospores are ellipsoidal of small diameter(80 ㎛). Because M5 was taxonomically similar to the Mucor circinelloides of zygomycetes, M5 was was identified and named as Mucor circinelloides M5. Bacteria B16 colony was opaque white, circular and lobate, and had rod shaped endospore. B16 was found positive in stain, catalase, β-glucosidse and V-P tests. B16 was found to utilize D-fructose, α-D-glucose, maltose, D-mannose, D-raffinose, stachyose and sucrose. By the morphological and physiological results, the characteristics of B16 was thought to correspond to that of Bacillus megaterium. However, fatty acid composition was similar to Paenibacillus marcerans, requiring further study for the definite identification. Accordingly, Bacteria B16 was provisionally classified and named as Bacillus megaterium B16.

전통메주로부터 Protease 생산 균주의 분리 , 동정 및 효소 생산조건

김성호,임무현,주현규,변영각,이갑상 한국농화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.5

A bacteria producing protease against soy protein was isolated from various traditional Me-Ju, in order to improve utililization and characteritics of soy protein hydrolysates reduced bitterness and advanced flavors. The optimal culture conditions for protease production was investigated. The isolated bacteria was identified as Bacillus subtilis by morphological and physiological charateristics and named Bacillus subtilis YG-95. The optimal culture condition of liquid medium for protease production by Bacillus subtilis YG-95 composed of 3.5% soluble starch, 3.0% soy protein isolate, 0.25%, dextrose, 0.5% NaCl, 0.25% K₂HPO₄ with on initial pH of 7.6, for 60 hrs at 45℃.

Bacillus subtilis YG-95 가 생산하는 protease 의 정제와 특성

김성호,임무현,주현규,변영각,이갑상 한국농화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.5

The protease produced by Bacillus subtilis YG-95 was purified by precipitating with ammonium sulfate, DEAF-sepharose 6B and Sephadex G-100 column chromatogtaphies and its purified enzymological characteritics were investigated. The molecular weight of purified protease was estimated about 43kilodalton by SDS PAGE The optimum pH and temperature for the purified protease activity were pH 10.0 and 55℃, respectively. The enzyme was stable in broad range of pH 5.0 to 12.0. and at the below 45℃. The purified enzyme activty was inhibited by Fe^(3+) and Al^(3+). The activity was significantly inhibited more than 80% by O-Phenanthroline, PMSF and SDS. The K_m value of the purified enzyme against Soy Protein Isolate as a substrate was 1.28 ㎎/㎖.