http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
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.
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.
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.
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.
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.
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.