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이은탁,강상구,Lee, Eun-Tag,Kang, Sang-Gu Korean Society of Life Science 2007 생명과학회지 Vol.17 No.6
A rice OsLeuD gene for small subunit of 3-isopropylmalate isomerase (IPMI) (EC 4.2.1.33) has been isolated. OsLeuD gene is located on 109.3 cM of chromosome 2. OsLeuD gene was expressed abundantly in metabolically active organs including leaves and developing seeds, indicating that OsLeuD gene expression is developmentally regulated. The cDNA of OsLeuD gene was coded for 257 amino acids which showed 58% and 48% homology to small subunits of IPMI in OsLeuD genes of cyanobacteria and green sulfur bacteria, respectively. The molecular character of OsLeuD is closely related to those of photosynthetic bacteria rather than those of eukaryotes including fungi and yeast. This suggests that OsLeuD gene in chromosomal genome of plants may possibly be originated from chloroplast genome. 식물의 루이신 생합성에 관여하는 3-isopropylmalate isomerase (IPMI) (EC 4.2.1.33) 효소의 소단편을 암호화는 Leucine D유전자를 벼로부터 분리하고 OsLeuD유전자로 명명하였다. OsLeuD유전자는 257개의 아미노산을 암호화하고 있으며 cyanobacteria의 IPMI 단백질과는 약58% 그리고 green sulfur bacteria들의 IPMI 단백질과는 약48%의 상동성을 갖고 있었다. 벼의 OsLeuD 유전자는 japonica벼 (Oryza sativa L.)의 2번 염색체의 26.45 Mb의 위치로서 109.3 cM 거리에 좌위하고 있었다. OsLeuD유전자는 잎과 성숙하는 종자에 많이 발현이 되었으므로 대사가 급증하는 발생단계 에 발현이 조절되는 것으로 여겨진다. OsLeuD유전자와 단백질은 균류와 yeast 보다 광합성 박테리아의 유전자와 높은 동질성을 보이는 것으로 보아 OsLeuD유전자는 식물의 엽록체 유전자 genome 에서 기원하여 핵 genome으로 이동 진화된 유전자로 추측된다.
한국재래간장 발효균 Bacillus subtilis K7 유래의 혈전용해 Protease의 정제 및 특성
김두영,이은탁,김상달,Kim, Doo-Young,Lee, Eun-Tag,Kim, Sang-Dal 한국응용생명화학회 2003 한국농화학회지 Vol.46 No.3
한국재래간장으로부터 혈전용해효소를 강하게 생산하는 균주를 선발하고 이를 Bacillus subtilis K7로 동정하였다. B. subtilis K7이 생산하는 혈전용해성 protease를 정제하여 분자량을 확인한 결과 21,500 Da이었다. 정제된 효소의 최적반응조건은 $40^{\circ}C$와 pH 9.0이었으며 pH 5.0라서 12.0까지 안정하고 $50^{\circ}C$에서 20분간 열처리한 후에도 50%이상의 효소활성을 가지며 EDTA, CDTA 및 iodoacetat에 실활하는 효소이었다. 이 효소의 fibrin에 대한 Km 값은 $1.8{\times}10^{-2}$ M이었다. An alkaline fibrinolytic protease-producing bacteria was isolated front Korean traditional soy sauce and identified as Bacillus subtilis K7 from the results of analyses of its morphological and physiological properties, $API^{\circledR}$, and Biolog system. The enzyme was purified by 75% ammonium sulfate fractionation, QAE-Sephadex anion and SP-Sephadex cation exchange column chromatography and Sephadex G-100 gel filtration. The specific activity of the purified enByme was 233.9 unit/mg protein and the yield of enzyme was 3.8%. The homogeneity of the purified enzyme was confirmed by polyacrylamide gel electrophoresis. Molecular mass of the enzyme was estimated about 21,500 Da by SDS-polyacrylamide get electrophoresis and gel chromatography. The optimum temperature and pH for the enzyme activity were $40^{\circ}C$ and 9.0, respectively. The enzyme was stable in a pH range of 5.0 to 12.0, and 60% of its activity was lost on heat treatment at $50^{\circ}C$ for 20 min. The activity of the purified enzyme was inhibited by the presence of $Fe^{2+},\;Ag^{2+},\;Cu6{2+}$, iodoacetate, ethylene diamine tetraacetic acid (EDTA), and trans-1,2-diaminocycloheane-N,N,N',N'-tetraacetic acid (CDTA). The results indicates that the enzyme requires a metal ion for its enzymatic activity.
생물방제균 Bfacillus subtilis YB-70의 외부 Urease 유전자 도입과 길항력 증강
최종규,김용수,이은탁,김상달,Choi, Jong-Kyu,Kim, Yong-Su,Lee, Eun-Tag,Kim, Sang-Dal 한국미생물 · 생명공학회 1997 한국미생물·생명공학회지 Vol.25 No.1
To genetically breed powerful multifunctional antagonistic bacteria, the urease gene of alkalophilic Bacillus pasteurii was transferred into Bacillus subtilis YB-70 which had been selected as a powerful biocontrol agent against root-rotting fungus Fusarium solani. Urease gene was inserted into the HindIII site of pGB215-110 and designated pGU266. The plasmid pGU266 containing urease gene was introduced into the B. subtilis YB-70 by alkali cation transformation system and the urease gene was very stably expressed in the transformant of B. subtilis YB-70(pGU266). The optimal conditions for the transfomation were also evaluated. From the in vitro antibiosis tests against F. solani, the antifungal activity of B. subtilis YB-70 containing urease gene was much efficient than that of the non-transformed strain. Genetic improvement of B. subtilis YB-70 by transfer of urease gene for the efficient control seemed to be responsible for enhanced plant growth and biocontrol efficacy by combining its astibiotic action and ammonia producing ability.
윤선주(Sun-Joo Youn),이은탁(Eun-Tag Lee),조준구(Jun-Gu Cho),김덕진(Duk-Jin Kim) 한국식품영양과학회 2010 한국식품영양과학회지 Vol.39 No.9
본 연구에서는 효소 처리에 의하여 제조한 천도복숭아 주스에 함유된 총 플라보노이드 함량은 대조구의 경우와 cellulase만을 처리한 처리구의 경우 각각 0.146 ㎎/mL, 0.148 ㎎/mL로 유사하였으나 pectinase만을 처리한 처리구와 pectinase와 cellulase를 혼합하여 처리한 처리구의 경우 각각 0.167 ㎎/mL와 0.171 ㎎/mL로 대조구보다 높게 나타났다. 항산화작용, 즉 전자공여능(DPPH) 조사한 결과는 효소처리구들이 대조구의 13.42%보다 높은 28.98% 이상으로 2배 이상의 활성을 나타나 효소처리에 의해 제조된 천도복숭아 주스가 열수추출에 의해 제조된 주스보다 높은 항산화기능이 유지될 수 있음을 유추할 수가 있었다. pH 조건별 아질산염 소거 효과를 비교하여 본 결과 대조구의 경우에서는 아질산염 소거능이 pH 1.2에서 약 79%로 나타났으나 효소처리구들은 90%를 이상의 결과들을 보였으며, pH 3.0, pH 4.0, pH 6.0에서도 대조구의 경우보다 높게 나타났다. 천도복숭아를 이용하여 제조한 주스의 유리아미노산 분석결과 aspartic acid, serine, alanine, GABA, glutamic acid가 총 유리아미노산 검출양의 86.71%에서 94.14% 범위로 대부분의 유리아미노산을 구성하는 것으로 검출되었으며, ornithine과 taurine 또한 검출이 되었다. 각종 무기원소 함량 조사의 결과는 질소성분(T-N)의 경우 대조구에 비해 효소처리구가 다소 높게 나왔으며, 인성분(P₂O?)의 경우는 대조구와 비슷한 결과를 보였으며, 칼슘성분(CaO)의 경우 45 ㎎/L 이상의 마그네슘성분(MgO)의 경우에서는 85 ㎎/L 이상의 농도를 보여 역시 높은 함유율을 보였으며, 칼륨성분(K₂O)의 경우에서는 2,133 ㎎/L 이상의 농도를 보여 역시 상당히 높은 함유율을 보였다. Nectarine beverage treated with cellulase and pectinase enzymes was measured for mineral contents, total flavonoids, and free amino acids and DPPH radical scavenging effect, nitrite scavenging effect. Total flavonoid contents of the no treatment, treated with pectinase, with cellulase, and with both measured 0.146 ㎎/mL, 0.167 ㎎/mL, 0.148 ㎎/mL and 0.171 ㎎/mL, respectively. DPPH was measured as 13.42% with no treatment and more than 28.98% with enzyme treatments. Nitrite scavenging effect with no treatment was 79% at pH 1.2. Whereas, it was measured above 90% while treated with enzymes at pH 1.2. And also, the nitrite scavenging effect was slightly higher at pH 3.0, pH 4.0 and pH 6.0 than no treatment. Results of free amino acids analysis revealed that, aspartic acid, serine, alanine, γ-aminobutylic acid, and glutamic acid were present with the amount ranging from 86.71% to 94.14% from total detected free amino acids. Ornithine and taurine were also observed from the beverages. The mineral contents, nitrogen element (T-N) of enzyme treatment of nectarine beverages were measured slightly higher than T-N of no treatment, however, the P₂O? was similar. Moreover, CaO, MgO and K₂O in the beverages were measured above 45 ㎎/L, 85 ㎎/L and 2,133 ㎎/L, respectively.
한국재래간장 발효균 Bacillus subutilis K7 유래의 혈전용해 Protease의 정제 및 특성
김두영 ( Kim Du Yeong ),이은탁 ( Lee Eun Tag ),김상달 ( Kim Sang Dal ) 한국응용생명화학회 2003 Applied Biological Chemistry (Appl Biol Chem) Vol.46 No.3
An alkaline fibrinolytic protease-producing bacteria was isolated from Korean traditional soy sauce and identified as Bacillus subtilis K7 from the results of analyses of its morphological and physiological properties. API^(?) and Biolog system. The enzyme was purified by 75% ammonium sulfate fractionation, QAE-Sephadex anion and Sp-Sephadex cation exchange column chromatography and Sephadex G-100 gel filtration. The specific activity of the purified enzyme was 233.9 unit/mg protein and the yield of enzyme was 3.8%. The homogeneity of the purified enzyme was confirmed by polyacrylamide gel electrophoresis. Molecular mass of the enzyme was estimated about 21.500 Da by SDS-polyacrylamide gel electrophoresis and gel chromatography. The optimum temperature and pH for the enzyme activity were 40℃ and 9.0. respectively. The enzyme was stable in a pH range 5.0 to 12.0 and 60% of its activity was lost on heat treatment at 50℃ for 20 min. The activity of the purified enzyme was inhibited by the presence of Fe^(2+), Ag^(2+), Cu^(2+), iodoacetate, ethylene diamine tetraacetic acid (EDTA), and trans-1.2-diaminocycloheane-N,N,N`,N`-tetraacetic acid (CDTA). The results indicates that the enzyme requires a metal ion for its enzymatic activity.