脫脂大豆粕에서 抽出한 分離大豆蛋白의 食品學的 性質

邊時明(Si-Myung Byun),金哲鎭(Chul-Jin Kim) 한국식품과학회 1977 한국식품과학회지 Vol.9 No.2

Lignin의 분해효소 및 이용

변시명,김현표,Byeon, Si-Myeong,Kim, Hyeon-Pyo 한국주류산업협회 1981 주류산업 Vol.1 No.1

Soyprotein Fiber Formation

변시명,권종훈,김철진,이양희,Byun, Si-Myung,Kwon, Jong-Hoon,Kim, Chul-Jin,Lee, Yang-Hee Korean Society of Food Science and Technology 1978 한국식품과학회지 Vol.10 No.2

저자들은 전보(Korean J. Food Sci. Techno., 9,123(1997)에서 분리 대두 단백의 식품학적 성질을 조사하였다. 본 연구에서는 이 성질을 응용하여 대두 단백섬유를 제조하고저 분실 험실에서 고안 설계하여 의뢰제작한 protein spinning apparatus를 사용하여 분리 대두단백으로 대두단백섬유 제조실험을 행한결과 texture가 우수한 제품을 얻었다. 제조조건은 15-18% 단백질용액을 알카리 (0.6%)로 처리하여 50-100 PSI spinning press로 사출한 후 12% Nacl-1 N acetic acid bath에서 응고시켰다. 12% 단백질 용액은 생성된 단백섬유의 texture가 불량하여 일정한 모형을 유지하지 못하였다. 제품의 성질을 Instron기기와 texturometer를 사용하여 측정하였다. 아울러 대두 단백섬유의 형성기작을 제시하였다. In our previous report (Korean J. Food Sci. Technol., 9, 123. (1977), functional properties of soyprotein isolates prepared from defatted soybean meal were studied. Using those properties soyprotein fibers, which may be acceptable as meat analogs, were prepared with protein spinning apparatus. Soyprotein can be converted into the suitable form for the spinning by denaturation with alkali (0.6%) and continuous fibers were spun by extruding spinning solution into an 20% NaCl-1 N acetic acid coagulating bath. The process for producing soyprotein fibers on a bench scale was described and break strength, break elongation and textural parameters of the fibers formed were evaluated. The possible scheme of formation of soyprotein fibers was discussed.

대두 Lipoxygenase 2 에 관한 연구

김길현,변시명 ( Kil - Hyun Kim,Si Myung Byun ) 생화학분자생물학회 1981 BMB Reports Vol.14 No.2

Soybean lipoxygenase 2 was purified by the combination of ammonium sulfate fractionation, affinity chromatography on linoleate-aminohexyl Sepharose 4 B and DEAE-cellulose chromatography. Purification of lipoxygenase 2 through affinity chromatography resulted in 6-fold purification and the yield of 91%, while lipoxygenase 1 was retrogressed and recovery was only 15%. Overall purification of lipoxygenase 2 was 32.4 folds and the yield was 28.5%, respectively. The purified enzyme preparation was almost homogeneous electrophoretically. When the lipoxygenase 2 preparation was incubated with arachidonic acid, and subsequently reduced with sodium dithionite, a material from ether extract of the reaction mixture seemed to have some of prostaglandin F_(2α), which was identified through thin layer chromatography.

무증자 전분의 당화에 관한 연구

김형수,변시명,Kim, Hyeong-Su,Byeon, Si-Myeong 한국주류산업협회 1984 주류산업 Vol.4 No.1

내산성 Glucoamylase 의 정제 및 특성에 관한 연구

김학주,변시명 ( Hack Joo Kim,Si Myung Byun ) 생화학분자생물학회 1977 BMB Reports Vol.10 No.3

An acid stable glucoamylase from Paecilomyces subglobosum was purified by affinity chromatography using the glycogen-Sepharose 4B gel in the single purification step. Glycogen was coupled to Sepharose 4B by the oxirane activation method and the gel absorbed 3.64 units of glucoamylase per gram of wet gel. The purified glucoamylase preparation showed a single protein band on 7% polyacryl amide gel by electrophoresis. Using this purified enzyme some kinetic parameters of the glucoamylase were studied. Km`s on starch and glycogen as substrates were 0.154 % and 0.125% respectively, the optimal pH 4.0, and the optimal temperature 55℃. The glucoamylase preparation was stable and showed 75 % activity even at pH 2.0 and was relatively stable by heat treatment.

Studies on Soybean Lipoxygenase 2

김길현,변시명,Kim, Kil-Hyun,Byun, Si-Myung 생화학분자생물학회 1981 한국생화학회지 Vol.14 No.2

Lipoxygenase 2 (E.C. 1. 13. 11. 12)를 대두로부터 친화성 크로마토그라피 방법과 DEAE-cellulose chromatography 방법으로 분리, 정제하였다. 친화성 크로마토그라파에서는 흡착제로서 linoleate-aminohexyl Sepharose 4B 를 사용하였으며, pH 6.8 에서 시행한 결과 lipoxygenase 2는 6배 정제되었고 수율은 91%였으나 lipoxygenase 1은 정제도가 오히려 떨어졌으며 수율은 15%이었다. 최종 lipoxygenase 2는 32.4 배 정제되었으며 수율은 28.5%이었다. 여기서 얻은 효소는 전기 영동법에 의해 거의 단일 단백질로 되어있음을 알 수 있었다. 여기서 얻은 lipoxygenase 2를 arachidonic acid와 반응 시킨후 sodium dithionite 로 환원시킨 다음 에테르로 추출한 물질중에 prostaglandin $F_{2{\alpha}}$로 보이는 소량의 물질이 포함되어 있음을 TLC 방법에 의해 확인하였다. Soybean lipoxygenase 2 was purified by the combination of ammonium sulfate fractionation, affinity chromatography on linoleate-aminohexyl Sepharose 4B and DEAE-cellulose chromatography. Purification of lipoxygenase 2 through affinity chromatography resulted in 6-fold purification and the yield of 91%, while lipoxygenase 1 was retrogressed and recovery was only 15%. Overall purification of lipoxygenase 2 was 32.4 folds and the yield was 28.5%, respectively. The purified enzyme preparation was almost homogeneous electrophoretically. When the lipoxygenase 2 preparation was incubated with arachidonic acid, and subsequently reduced with sodium dithionite, a material from ether extract of the reaction mixture seemed to have some of prostaglandin $F_{2{\alpha}}$, which was identified through thin layer chromatography.

내산성 Glucoamylase의 정제 및 특성에 관한 연구

김학주,변시명,Kim, Hack-Joo,Byun, Si-Myung 생화학분자생물학회 1977 한국생화학회지 Vol.10 No.3

Paecilomyces subglobosum이 생산하는 내산성 glucoamylase(EC. 3. 2. 1. 3)를 glycogen-Sepharose 4B affinity chromatography에 의하여 1단계 작업으로 정제하였다. Glycogen-Sepharose 4B는 Sepharose 4B를 oxirane으로 activation 시킨후 글리코겐을 결합시켰으며 이 gel은 wet gel g 당 최소한 3.64 units의 glucoamylase를 흡착하였다. 정제한 glucoamylase는 7% polyacryl amide gel 전기영동상에서 단일대를 보여주었다. 정제한 glucoamylase의 Km은 전분과 글리코겐에 대하여 각기 0.154%, 0.125%였으며 이 효소의 최적 pH는 4.0, 최적온도는 $55^{\circ}C$이었다. Glucoamylase는 pH 2에서도 75%의 효소역가를 보여주었고 낮은 pH와 열에 대한 안정성도 비교적 양호하였다. An acid stable glucoamylase from Paecilomyces subglobosum was purified by affinity chromatography using the glycogen-Sepharose 4B gel in the single purification step. Glycogen was coupled to Sepharose 4B by the oxirane activation method and the gel absorbed 3. 64 units of glucoarnylase per gram of wet gel. The purified glucoamylase preparation showed a single protein band on 7% polyacryl amide gel by electrophoresis. Using this purified enzyme some kinetic parameters of the glucoamylase were studied. Km's on starch and glycogen as substrates were 0.154% and 0.125% respectively, the optimal pH 4.0, and the optimal temperature $55^{\circ}C$. The glucoamylase preparation was stable and showed 75% activity even at pH 2.0 and was relatively stable by heat treatment.

Nonenzymatic Cleavage of Escherichia coli Glutamine Synthetase by Dithiothreitol and Iron(III)

전덕영,김강화,변시명,Jhon, Deok-Young,Kim, Kang-Hwa,Byun, Si-Myung 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.4

대장균 글루타민 합성효소에 대한 디티오트레이톨과 철 (III)이온에 의한 비효적 절단반응의 최적조건은 이 효소의 농도가 단량체로서 0.06 mM 일 때 디티오트레이톨 5 mM, 철 (III) 0.1 mM, pH 7.0, $37^{\circ}C$, 반응시간은 4시간이었다. 절단양상은 기질 및 기질유사체인 글루타민, 글루타민산, L-메치오닌 술폭시민 등 리간드의 첨가에 의하여 크게 변화되었다. 그러나 이들 화합물은 동일한 절단조건에 의해서 절단되는 피루브산 키나제에 대해서는 그 고유한 절단양상을 변화시키지 않았다. 이들 결과는 대장균 글루타민 합성효소의 디티오트레이톨과 철 (III) 이온에 의한 절단이 효소의 활성부위에서 일어남을 시사한다. Optimum reaction condition for the cleavage of Escherichia coli glutamine synthetase in the presence of oxygen, iron(III), and dithiothreitol has been established. The condition is 5 mM dithiothreitol, 0.1 mM iron(III), pH 7.0,$37^{\circ}C$, and 4hours of reaction time, when the enzyme concentration is 0.06 mM as subunit basis. The cleavage pattern strongly depends on the addition of ligands of the enzyme, glutamic acid, glutamine, L-methionine-S-sulfoximine, to the reaction mixture while the ligands do not change the cleavage pattern of rabbit muscle pyruvate kinase which is also attacked by the cleavage system. The results indicate that the cleavage reaction occurrs at the polypeptide segments which consist the active site of the glutamine synthetase.

Urokinase Conjugated with Water-Soluble Dextran

김남득,김현표,변시명,김성완,Kim Nam Deuk,Kim Hyun-Pyo,Byun Si Myung,Kim Sung Wan Korean Chemical Society 1985 Bulletin of the Korean Chemical Society Vol.6 No.4

Urokinase, a plasminogen activator, was conjugated with dextran by the cyanogen bromide activation-coupling method. The resulting water-soluble conjugate was purified by gel permeation chromatography on Sephadex G-200. The maximal activity was obtained when the ratio of urokinase/dextran was 1/20 for the coupling. The final preparation showed 5 CTA units/mg conjugate, 300 CTA units/mg protein, 8.4 % activity retention, and 47 % protein retention. The urokinase-dextran conjugate had good thermal, pH and storage stabilities. In addition, it showed greater resistance to the inhibitory effect of human plasma than native urokinase. Also in vitro biological half-life of urokinase increased 40 times by this conjugation. In view of activity, excellent stability and increased half-life, the conjugate can be a potential fibrinolytic agent in an injectable form.