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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.
Aspergillus속 균주가 생산하는 Phytase의 분리 정제 및 특성
천성숙(Sung-Sook Chun),조영제(Young-Je Cho),차원섭(Woen-Suep Cha),이희덕(Hee-Duck Lee),이선호(Sun-Ho Lee),최청(Chung Choi) 한국식품영양과학회 1998 한국식품영양과학회지 Vol.27 No.1
단백질과 결합하여 단백질의 용해도를 저하시키고, 무기질의 흡수를 저해하는 phytic acid의 효소에 의한 분해, 제거를 목적으로 phytase를 생산하는 Aspergillus sp. SM-15 균주를 토양으로 부터 분리하고 이 균주가 생산하는 효소를 정제하여 특성을 규명하였다. Phytase생산조건을 밀기울배지에 1.0% mannose, 2% yeast extract, 0.5% (NH₄)₂HPO₄, 0.2% calcium chloride를 첨가하여 4일 배양시 최대 활성을 나타내었다. 효소는 ion exchange chromatography, gel filtration 등으로 약 17.1배 정제하였고 효소의 비활성역가는 244.32unit/㎎이었다. 정제효소는 polyacrylamide gel 전기영동상 단일밴드로 나타났으며, 분자량은 46,000 전도로 추정되었다. 정제효소의 특성은 최적 pH와 온도는 각각 5.0, 50℃였으며, 안정범위는 pH 4.5~5.5까지 였다. 금속이온 중 Fe^(2+), Pb^(2+) 등에 의해 활성이 증대되었으나, Hg^(2+)에 의해 효소활성이 저해되었고, 저해제 중 iodine에 의해서 활성저해가 관찰되어 active site에 histidine 잔기가 존재하는 것으로 추정되었으며, 정제효소의 Km과 Vmax는 각각 37.037mM/L, 159.87μ㏖/min이었다. To extract insoluble proteins and to improve funtional properties of abolished proteins, an phytase producing Aspergillus sp. SM-15 was isolated from soil. The enzyme was purified and its enzymological characteristics were investigated. Phytase production reached to maximum when the wheat bran medium containing 1% mannose, 1% yeast extract, 1% (NH₄)₂HPO₄ and 0.2% calcium chloride was cultured for 4 days. Phytase was purified 17.1 fold and specific activity was 244.32unit/㎎ by a sequencial precess of ammonium sulfate fraction, ion exchange chromatography and gel filtration. Purified enzyme was confirmed as a single band by the polyacrylamide gel electro-phoresis. The molecular weight of phytase was estimated to be 46,000. The optimum pH and temperature for the phytase activity were 5.5 and 50℃. The enzyme is stable in pH 4.5~5.5, 60℃. The activity of purified enzyme was inhibited by Hg^(2+) whereas activited by Pb^(2+) and Fe^(2+). The activity of phytase was inhibited by the treatment with iodine. The result indicate the possible involvement of histidine at active site. Km and Vmax of the purified phytase were 37.037mM/L and 159.87μ㏖/min, respectively.
Phytase 처리에 의한 폐단백자원의 단백질 용출 및 기능성 변화
천성숙(Sung-Sook Chun),조영제(Young-Je Cho),김영활(Young-Hwal Kim),우희섭(Hi-Seob Woo),최청(Chung Choi) 한국식품영양과학회 1998 한국식품영양과학회지 Vol.27 No.1
폐단백질을 활용하는 방도의 하나로 폐단백질자원으로부터 토양에서 분리한 Aspergillus sp. 균주가 생산하는 phytase를 이용하여 불용성 단백질의 분리 효율성을 높였으며 추출 단백질의 기능성을 살펴보았다. 참깨박에 함유되어 있는 불용성 형태의 단백질을 가용성 형태의 단백질로 용출시키기 위한 최적 pH, 최적 온도, 최적 처리시간과 최적 첨가효소량은 4.0~5.0, 50℃, 8~10시간, 120unit였고, 효소처리된 참깨박은 phytase 처리의 경우 대조구에 비해 기포형성력은 크게 증가하지 않았으나 기포안정성은 다소 증가하였다. 참깨박 단백질의 유화력은 다소의 유화력과 안정성의 증가가 관찰되었고, 유지흡착력과 수분흡착력은 대조구에 비해서 높은 값을 나타내었다. This study was performed to improve extraction of insoluble proteins and to evaluate funtional properties of abolished proteins by the phytase produced by Asporgillus sp. The optimum pH, temperature, treatment time and unit of the enzyme for extraction of protein were pH 4.0~5.0, 50℃, 8~10hrs and 120 units. The foaming capacity and foaming stability of sesame meal protein after enzyme treatment were virtually unchanged as compared to control. The emulsion capacity and emulsion stability of sesame meal protein was higher than control. Oil 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.
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.
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.