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Protease 처리에 의한 폐단백자원의 단백질 용출 및 기능성 변화
천성숙,조영제,손규목,최희진,최청 ( Sung Sook Chun,Young Je Cho,Gyu Mok Son,Heui Jin Choi,Cheong Choi ) 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.1
To improve extraction of insoluble proteins and functional properties of abolished proteins by protease. It was found that the optimum pH, optimum temperature, optimum treatment time and optimum unit of enzyme far extraction of protein were pH 9.0, 60℃, 8 hrs, 40 units. The foaming capacity and foaming satbility of sesame meal protein after treatment of enzyme were especially higher than control. The emulsion capacity and emulsion satbility of sesame meal protein were higher than control. Coil absorption as well as water absorption capacities of sesame meal protein were higher than control.
폐단백자원에 이용하기 위한 미생물 Protease 의 특성
천성숙,조영제,성태수,손준호,최청 ( Sung Sook Chun,Young Je Cho,Tae Soo Sung,Jun Ho Son,Cheong Choi ) 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.1
To extract insoluble proteins and to improve functional properties of abolished proteins, a protease producing Aspergillus sp. MS-18 was isolated from soil. The enzyme was purified and its enzymological characteristics were investigated. It was found that production of protease reached to the maximum when the wheat brae medium containing, 3% arabinose, 0.5% polypepton, 0.1% (NH₄)₂SO₄ and 0.2% magnesium chloride was cultured for 3 days. Protease was purified 16.9 folds after ion exchange chromatography and gel filtration and the specific activity was 340.4 unit/㎎. Purified enzyme was confirmed as a single band by the polyacrylamide gel electrophoresis. The molecular weight of protease was estimated to be 30,000. Crystalization form of purified protease was a stick shape with rounding edges. The optimum pH and temperature for the protease activity were 9.0 and 60℃, respectively. The enzyme was stable in pH 7.0-12.0 at 50℃. The activity of purified enzyme was inhibited by Hg^(2+), Zn^(2+) and Pb^(2+), whereas it was activited by Na^+, Mg^(2+) and Mn^(2+). The activity of the protease was inhibited by the treatment with ethylenediaminetetraacetic acid and phenylmethane sulfonyl fluoride. The result suggests that the purified enzyme is a serine protease with metal ion at active site. Km and Vmax of purified protease were 29.33 μmole/L and 5.13 ㎍/min, respectively.
한국산 대추의 Endo - Polygalacturonase 의 특성
최청 ( Cheong Choi ),천성숙 ( Sung Sook Chun ),조영제 ( Young Je Cho ),안봉전 ( Bong Jeon Ahn ),김영활 ( Young Hwal Kim ),이선호 ( Seon Ho Lee ),김성 한국응용생명화학회 1994 Applied Biological Chemistry (Appl Biol Chem) Vol.37 No.5
The optimum pH and temperature for endo-polygalacturonase activity from Jujube were 5.0 and 50℃. The range of its stability to pH was 4.0 to 5.0. The enzyme was inactivated about 35% by treatment at 70℃ for 1 hr. It was found that Ag^+, Zn^(++) and Mg^(++) increased the enzyme activity. In contrast, Ba^(++), Hg^(++), Pb^(++), Ca^(++), Mn^(++), Cu^(++), Fe^(++), Na^+ and K^+ decreased it. The enzyme was inactivated by treatment with malefic anhydride, iodine and 2,4-dinitrophenol. The results indicate that active site is a imidazole group on the enzyme.
한국산 대추로부터 Endo - polygalacturonase 분리 및 정제
최청(Cheong Choi),천성숙(Sung Sook Chun),조영제(Young Je Cho),우희섭(Heui Seob Woo),김태완(Tae Wan Kim),허영훈(Young Hoon Heo) 한국응용생명화학회 1994 Applied Biological Chemistry (Appl Biol Chem) Vol.37 No.4
Endo-polygalacturonase was purified from Jujube. The purification procedures included DEAE-cellulose ion exchange chromatography and gel filteration on Sephdex G-100. Enzyme was purified as a single protein band and purification yield was about 6%. When the purified enzyme was applied to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular weight was estimated about 19,000. Purified enzyme formed hexagonal board type.
Pseudomonas sp . SJ - 320 로부터 알칼리성 단백질 가수분해효소의 생산과 특성
최정,김영활,천성숙 ( Cheong Choi,Sung Sook Chun,Yung Hawr Kim ) 생화학분자생물학회 1993 BMB Reports Vol.26 No.6
An alkaline protease producing microorganism was isolated from soil and identified as Pseudomonas sp. SJ-320. The optimum cultivation condition of Pseudomonas sp. SJ-320 for the production of alkaline protease was as follow; 1.0% casein, 0.2% ammonium chloride, 0.2% NaH₂PO₄, 1.0% fructose, 20℃, pH 10.0 and 140 h. The optimum pH and temperature for the enzyme activity were pH 8.0 and 50℃, respectively. The enzyme was relatively stable at pH 7.5∼8.5 and at temperature below 50℃. The activity of the partially purified enzyme was inhibited by He^(2+) and Cu^(2+) whereas Mn^(2+), Mg^(2+) and Ca^(2+) gave rather activating effects on the enzyme activity. ε-Aminocaproic acid and 2,4-dinitrophenol did not inhibit the enzyme, but p-chloromercuribenzoic acid and ethylendiaminetetraacetic acid inhibited the enzyme activity, indicating that reactive sulfhydryl group and metal ion group are required for the enzyme activity. The enzyme was resistant to various detergents, except for sodium dodecyl sulfate.
Pseudomonas sp. SJ-320로부터 알칼리성 단백질 가수분해효소의 생산과 특성
최청,김영활,천성숙,Choi, Cheong,Chun, Sung-Soak,Kim, Yung-Hawr 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.6
알칼리성 단백질 가수분해효소의 생산능력이 강한 Pseudomoηas sp. SJ-320을 토양으로부터 분리하였으며 효소생산의 최적 배양조건은 배지에 1% casein, 0.2% ammonium chloride, 0.2% $NaH_{2}PO_{4}$, 1% fructose를 혼합첨가하여 $20^{\circ}C$, pH 10.0에서 6일간 배양하였을 때 효소생산이 최대로 나타났다. 효소의 최적 작용 pH와 온도는 pH 8.0, $50^{\circ}C$ 였으며, pH 7.5-8.5의 범위와 $50^{\circ}C$ 이하에서 안정하였다. 급속이온 중 $Mn^{2+}$, $Mg^{2+}$과 $Ca^{2+}$ 등에 의하여 활성이 증대되었으나 $Hg^{2+}$, $Cu^{2+}$ 등에 의하여 효소활성이 저해되었다. 2,4-dinitrophenol, ${\varepsilon}-aminocaproic$ acid 처리에 의해 활성이 저해되지 않았으나 ethylenediaminetetraacetic acid와 p-chloromercuribenzoic acid에 의해 활성이 저해되어 효소분자 중 sulfhydryl기가 활성에 어느 정도 관여하는 metallo enzyme으로 추정되였다. 이 효소는 sodium dodecyl sulfate을 제외한 여러 가지 계면활성제에 대해서 강한 저항성을 가지고 있었다. An alkaline protease producing microorganism was isolated from soil and identified as Pseudomonas sp. SJ-320. The optimum cultivation condition of Pseudomonas sp. SJ-320 for the production of alkaline protease was as follow; 1.0% casein, 0.2% ammonium chloride, 0.2% $NaH_{2}PO_{4}$, 1.0% fructose, $20^{\circ}C$, pH 10.0 and 140 h. The optimum pH and temperature for the enzyme activity were pH 8.0 and $50^{\circ}C$, respectively. The enzyme was relatively stable at pH 7.5-8.5 and at temperature below $50^{\circ}C$. The activity of the partially purified enzyme was inhibited by $Hg^{2+}$ and $Cu^{2+}$ whereas $Mn^{2+}$, $Mg^{2+}$ and $Ca^{2+}$ gave rather activating effects on the enzyme activity. ${\varepsilon}-Aminocaproic$ acid and 2,4-dinitrophenol did not inhibit the enzyme, but p-chloromercuribenzoic acid and ethylendiaminetetraacetic acid inhibited the enzyme activity, indicating that reactive sulfhydryl group and metal ion group are required for the enzyme activity. The enzyme was resistant to various detergents, except for sodium dodecyl sulfate.
한국산 녹차로 부터 분리한 축합형 탄닌의 Xanthine Oxidase 저해효과
조영제(Young-Je Cho),천성숙(Sung-Sook Chun),최청(Cheong Choi) 한국식품영양과학회 1993 한국식품영양과학회지 Vol.22 No.4
기능성 식품과 생약재료의 이용을 위한 연구의 일환으로 한국산 녹차로 부터 탄닌을 분리하여 xanthine oxidase 저해효과를 측정하였다. 녹차의 acetone 추출물에서 xanthine oxidase 저해효과가 있음이 확인되었고 정제된 탄닌의 효소 저해효과를 검토한 결과 xanthine oxidase 저해의 경우 galloyl tannin류가 nongalloyl tannin류보다 활성이 더 우수하였고 구조적 이성체에서도 (+)-catechin류 보다 (-)-epicatechin류가 효소저해 효과가 더 좋았으며, 각 물질간 상승 효과가 인정되었다. 녹차에서의 탄닌류는 xanthine oxidase에 대해 비경쟁적 저해를 하는 것을 알 수 있었다. For the purpose of utilizing tannins in the functional foods and crude drugs the xanthine oxidase inhibition of tannins isolated from Korean green tea was determined. Acetone extract from Korean green tea showed inhibitory effect against the xanthine oxidase. The galloyl tannins showed higher inhibitory activity against xanthine oxidase than the nongalloyl tannins. In terms of stereo isomers, (-)-epicatechins had higher inhibitory activity than the (+)-catechins. The synergistic activity was also observed. Tannins isolated from Korean green tea appeared to be incompetitive inhibitor against the xanthine oxidase.
Rhizopus oryzae CJ - 2114가 생성하는 Polygalacturonase의 특성 및 작용양상
정영건(Yung-Gun Chung),조영제(Young-Je Cho),천성숙(Sung-Sook Chun),최청(Cheong Choi) 한국식품영양과학회 1992 한국식품영양과학회지 Vol.21 No.2
Rhizopus oryzae CJ-2114 가 생성하는 polygalacturonase의 최대활성을 위한 pH는 4.0, 최적온도는 40℃였으며, 효소활성화 에너지는 2.049Kcal/㏖ 이었다. 정제효소의 Km 값과 V_(max) 값은 54.05mM, 13.9m mole/min 이었고, pectin보다 polygalacturonic acid를 특이적으로 분해하였다. 이 효소는 약산성의 pH에서 안정성을 보였으며, 온도에 의한 안정성은 40℃였으며, 50℃ 이상에서는 급격한 효소단백질의 불활성화가 진행되었다. 금속이온중 Na^+ 이온에 의해 활성이 유지되며 Cu^(2+), Pb^(2+), Mn^(2+), Zn^(2+) 이온 등은 효소활성을 저해하였다. 효소저해제 중 maleic anhydride와 iodine 등에 의해 효소활성이 저해되어 효소분자중의 histidine의 imidazole기와 cystein의 SH기가 효소활성에 관여함이 입증되었다.<br/> 이 효소의 기질분해양상을 여지 크로마토그라피로 확인한 결과 반응초기에는 monomer, dimer, oligomer 등이 생성되었고, 시간이 경과할수록 oligomer는 사라지고 monomer, dimer만이 생성되는 것으로 보아 endo 형인 것으로 판단되었으며, 효소의 과즙청정도 측정에서는 약 18.2×10³ unit 에서 거의 청정화 되었다 . Rhizopus oryzae CJ-2114 was selected for its strong polygalacturonase activity among various strains of mold found in soil. The optimum pH for the enzyme activity was 4.0 and optimum temperature was 40℃. The activation energy for the polygalacturonase was calculated by Arrhenius equation was 2.048Kcal/㏖. The reaction of this enzyme followed typical Michaelis-Menten kinetics with the Km value of 54.05mM with the V_(max) of 13.9m mole/min. The enzyme is relatively stable in acidic condition. The activity of polygalacturonase was inhibited completely by Cu^(2+), Pb^(2+), Zn^(2+) and Mn^(2+) at concentration of 1mM. The enzyme can be inactivated by the treatment with maleic anhydride and iodine. The results indicate the possible involvement of histidine at active site. When polygalacturonase from Rhizopus oryzae CJ-2114 was reacted with polygalacturonic acid as a substrate mono-, di-, and oligogalacturonic acid were produced at early and mono-, digalacturonic acid produced at late incubation time.