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Rhizobium japonicum 1-23 Glutamine Synthetase I의 분리 정제 및 성질
이왕식,성하진,방원기,Lee, Wang-Sik,Sung, Ha-Chin,Bang, Won-Gi 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.4
Glycerol를 유일한 탄소원으로 하여, Rhizobium japonicum 1-23으로부터, Glutamine synthetase I (GS I)을 유도하였다. 이 효소를 열처리, 황산암모니움 분별침전, DEAE-Sepharose 음이온 교환, Cibacron Blue F3GA affinity chromatography 및 Ultrogel AcA 22 gel fractionation 과정을 통하여 28.8배 정제하였다. 정제된 GS I의 $\bar{n}$은 4.5이었으며, isoactivity point는 7.53이었다. GS I은 크기가 52,000인 동일한 12개의 subunit으로 구성되어 있는 전체 분자량 약 600,000으로 추정되었다. GS I의 활성은 7.14 mM의 alanine에 의하여 87.2%가 저해되었으며, 5 mM의 inosine에 의하여 98.1%가 저해 되었다. Glutamine에 대한 $K_m$값은 5.4 mM이었으며, $V_{max}$는 $6.90{\mu}mol/min/mg$이었다. Glutamine synthetase I (GS I) was induced in Rhizobium japonicum 1-23 grown on glycerol as a sole source of carbon. The enzyme was purified 28.8 fold by heat-treatment ammonium sulfate fractionation, DEAE-Sepharose ion-exchange chromatography, Cibacron-Blue F3GA affinity chromatography, and Ultrogel AcA 22 gel fractionation. The $\bar{n}$ and the isoactivity point of GS I were 4.5 and 7.53, respectively. Molecular weight of GS I was 600,000 composed of twelve identical 52,000 subunits. The activities of GS I were inhibited by 87.2% (7.14 mM of alanine) and 98.1% (5 mM of inosine). $K_m$ for the substrate, glutamine, was 5.4 mM and $V_{max}$ was $6.90{\mu}mol/min/mg$.
Rhizobium Japonicum 1 - 23 Glutamine Synthetase Ⅰ의 분리 정제 및 성질
이왕식,성하진,방원기 ( Wang Sik Lee,Ha Chin Sung,Won Gi Bang ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.4
Glutamine synthetase I (GS I) was induced in Rhizobium japonicum 1-23 grown on glycerol as a sole source of carbon. The enzyme was purified 28.8 fold by heat-treatment ammonium sulfate fractionation, DEAE-Sepharose ion-exchange chromatography, Cibacron-Blue F3GA affinity chromatography, and Ultrogel AcA 22 gel fractionation. The n and the isoactivity point of GS I were 4.5 and 7.53, respectively. Molecular weight of GS I was 600,000 composed of twelve identical 52,000 subunits. The activities of GS I were inhibited by 87.2% (7.14 mM of alanine) and 98.1% (5 mM of inosine). K_m for the substrate, glutamine, was 5.4 mM and V_(max) was 6.90 μ㏖/min/㎎.
Candida sp . BT001 의 xylose reductase 의 정제 및 성질
이왕식,방원기,황인균,이상협 한국농화학회 1993 Applied Biological Chemistry (Appl Biol Chem) Vol.36 No.3
Xylose reductase (alditol: NADP^+ 1-oxidoreductase, EC 1.1.1.21) from the xylosefermenting yeast, Candida sp. BT001, was purified via salt fractionation, ion-exchange, gel filtration and affinity chromatography, and its properties were characterized. The enzyme from the yeast was active with both NADPH and NADH as coenzyme. The xylose reductase activity with NADH was approximately 51% of that with NADPH and the specific activities of purified enzyme with NADPH and NADH were 11.78 U/㎎ and 6.01 U/㎎, respectively. Molecular weight of the purified enzyme was 31,000 on SDS-PAGE and 61,000 on gel filtration. The Km for D-xylose, NADPH, and NADH was 94.2×10^(-3)M, 0.011×10^(-3)M, and 0.032×10^(-3)M, respectively. The purified xylose reductase had relatively higher substrate affinity for L-arabinose than other aldoses tested. The optimal pH was 6.2 and the optimal reaction temperature was 45℃. The thermal stability of the enzyme was for 20 minutes at 30℃.
Saccharomyces sake KBA No . 6 에 의한 Ergosterol 의 생산
이왕식,방원기,박장우 한국농화학회 1990 Applied Biological Chemistry (Appl Biol Chem) Vol.33 No.1
To produce ergosterol Saccharomyces sake KBA No. 6 was used and various factors related to ergosterol accumulation were investigated. The most effective inorganic nitrogen source was ammonium chloride and 3.50 % of ergosterol was accumulated in the cell when the C/N ratio was 200/1. When Tween 80 and potassium nitrite were used simultaneously, ergosterol content and total amount of ergosterol were increased by 56 % and 45 %, respectively, compared to their control in which 0.2 % of Tween 80 and 0.1 % of potassium nitrite were used. Under the optimum conditions, ergosterol content increased from 1.73 % to 5.3 % and the total amount of ergosterol was increased from 65.2 ㎎/1 to 135.15 ㎎/1.
이윤동,이왕식,방원기 한국농화학회 1988 Applied Biological Chemistry (Appl Biol Chem) Vol.31 No.4
The optimal reaction conditions were investigated to produce L-phenylalanine from transcinnamic acid and ammonia by Rhodotorula glutinis IFO 0559. The highest amount of L-phenylalanine was produced when the reaction mixture containing 200mM of traps-cinnamic acid, 4M of NH₄OH, 250mM of (NH₄)₂SO₄ 0.005% of cetylpyridinium chloride (pH 10.5) and 50㎎/㎖ of dry cell was used. Among the nonaqueous organic solvents, petroleum ether was the most effective on the production of L-phenylalanine. The optimal concentration of petroleum ether in the reaction mixture was 50%. Under the optimal conditions, 21.1g/ℓ of L-phenylalanine was produced in 12hr, and the yield was 63.9% based on transcinnamic acid.