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한국재래간장으로 부터 분리한 Bacillus subtilis CCKS - 111이 생성하는 Protease의 특성 및 작용양상
최청(Cheong Choi),최광수(Kwang-Soo Choi),조영제(Young-Je Cho),임성일(Sung-Il Lirn),김성(Sung Kim),손준호(Jun-Ho Son),이희덕(Hee-Duck Lee),김영활(Young-Hwal Kim) 한국식품영양과학회 1996 한국식품영양과학회지 Vol.25 No.6
한국재래간장으로부터 분리한 Bacillus subtilis CCKS-111이 생성하는 protease 생산의 최적 배양조건은 2% soluble starch, 0.2% peptone, 0.1%(NH₄)₂S₂O_8, 0.2% MgSO₄, pH 7.0, 35℃에서 24시간 배양했을 때이다. 효소의 최적작용 pH와 온도는 pH 9.0, 50℃였으며, pH 6.0~11.0의 범위와 50℃ 이상에서 불안정하였다. 금속이온 중 Cu^(2+)에 의하여 활성이 증대되었으나 K^(2+), Hg^(2+)등에 의하여 효소활성이 저해되었다. Ethylenediaminetetraacetic acid와 phenylmethane sulfonyl fluoride 처리에 의해 활성이 저해되어 금속이온의 영향을 받는 serine protease로 확인되었다. Km값은 2.313×10^(-4)M, V_(max)값은 39.216㎍/min이었으며, hemoglobin보다 casein을 더 잘 가수분해하였다. An alkaline protease producing microorganism was isolated from Korean traditional soy sauce and identified as Bacillus subtilis CCKS-111. The optimum culture condition of Bacillus subtilis CCKS-111 for the production of alkaline protease was as follow: 2% soluble starch, 0.2% peptone, 0.1% (NH₄)₂S₂O_8, 0.2% MgS0₄, pH 7.0, 35℃ and 24hrs. The optimum pH and temperature for the enzyme activity of alkaline protease producing Bacillus subtilis CCKS-111 were pH 9.0 and 50℃, respectively. The enzyme was relatively stable at pH 6.0~11.0 and at temperature below 40℃. The activity of the enzyme was inhibited by K^+ and Hg^(2+), whereas Cu^(2+) exhibited rather activating effects on the enzyme activity. Ethylenediaminetetraacetic acid and phenylmethanesulfonyl fluoride inhibited the enzyme activity. This indicates that this is serine protease which requires metal ion group for the enzyme activity. Km value was 2.313×10^(-4)M/L, V_(max) value was 39.216㎍/min. This enzyme hydrolyzed casein more rapidly than the hemoglobin.
한국재래간장으로 부터 분리한 Bacillus subtilis CCKS-111이 생성하는 Protease의 분리 및 정제
김성,임성일,이희덕,이선호,손준호,최희진,김영활,최청,Kim, Sung,Lim, Seong-Il,Lee, Hee-Duck,Lee, Seon-Ho,Son, Jun-Ho,Choi, Hee-Jin,Kim, Yeung-Hweal,Choi, Cheong 한국응용생명화학회 1997 Applied Biological Chemistry (Appl Biol Chem) Vol.43 No.2
한국재래간장으로 부터 분리한 Bacilius subtilis CCKS-111이 생성하는 proteae를 분리 정제하였다. 황산암모늄 염석, DEAE cellulose ion-exchange chromatography, Sephades G-100 및 HPLC를 이용한 겔여과법에 의해 비활성도 24.3 unit/mg, 정제배수 50.6배로 효소를 정제하였으며 high performance liquid chromatography (HPLC)에 의하여 단일 단백질임을 확인하였다 정제효소의 분자량은 HPLC에 의하여 분자량 28,000 정도의 monomer로 추정되었고, 본 효소의 아미노산 잔기수는 251.3으로, 분해되기 쉬운 threonine, serine, glycine을 제외한 아미노산 잔기수는 Bacillus subtilis subtilisin DY 잔기수(274)와 유사한 것으로 나타났다. 아미노산 조성은 alanine, serine, glycine 및 arginine의 함량이 많았다. Reverse phase (RP)-HPLC로 분리한 주 peak로 N-말단에서 32번 까지 아미노산 배열을 확인한 결과 Bacillus subtilis subtilisin DY와 동일하였다. A protease was purified from Bacillus subtilis CCKS-111 by ammonium sulfate treatment, DEAE-cellulose ion-exchange chromatography, Sephadex G-100 gel filtration and high performance liquid chromatography (HPLC). The specific activity of the purified enzyme was 24.3 unit/mg protein and the purification fold of enzyme was 50.6. Molecular weight of the purified enzyme estimated about 28,000 by HPLC gel filtration. The amino acid residues of this enzyme were 251.3 except threonine, serine and glycine. This result was similar to Bacillus subtilis subtilisin DY. From the first N-terminal amino acid to the 32th amino acid, the amino acid sequence was estimated after RP-HPLC elution. N-terminal and the 32th amino acids were alanine and aspartic acid. Alanine, serine, glycine and arginine were four major acids in the enzyme.
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.
한국재래간장으로 부터 분리한 Bacillus subtilis CCKS-111이 생성하는 Protease의 분리 및 정제
최청,김성,임성일,이희덕,이선호,손준호,최희진,김영활 ( Cheong Choi,Sung Kim,Seong Il Lim,Hee-Duck Lee,Seon Ho Lee,Jun Ho Son,Hee Jin Choi,Yeung hweal Kim ) 한국응용생명화학회 1997 Applied Biological Chemistry (Appl Biol Chem) Vol.40 No.3
A protease was purified from Bacillus subtilis CCKS-111 by ammonium sulfate treatment, DEAE-cellulose ion-exchange chromatography, Sephadex G-100 gel filtration and high performance liquid chromatography (HPLC). The specific activity of the purified enzyme was 24.3 unit/㎎ protein and the purification fold of enzyme was 50.6. Molecular weight of the purified enzyme estimated about 28,000 by HPLC gel filtration. The amino acid residues of this enzyme were 251.3 except threonine, serine and glycine. This result was similar to Bacillus subtilis subtilisin DY. From the first N-terminal amino acid to the 32th amino acid, the amino acid sequence was estimated after RP-HPLC elution. N-terminal and the 32th amino acids were alanine and aspartic acid. Alanine, serine, glycine and arginine were four major acids in the enzyme.
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.
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.
Bacillus licheniformis CN - 115 균주를 이용한 청국장 제조 과정에 있어서 단백질 및 아미노산의 변화
석영란(Yeong Ran Seok),김영활(Yung Hawl Kim),김성(Sung Kim),우희섭(Hi Seob Woo),김태완(Tae Wan Kim),이선호(Son Ho Lee),최청(Cheong Choi) 한국응용생명화학회 1994 Applied Biological Chemistry (Appl Biol Chem) Vol.37 No.2
Chungkook-Jang was produced by fermenting Bacillus licheniformis CN-115. The changes of chemical composition, enzyme activity, and amino acids during the fermentation were investigated. The proximate composition was shown irregular fluctuation phenomenon during the fermentation, but only the moisture tended some reducing during the fermentation just after steaming. The content of amino nitrogen was increased radically after the 36 hours of fermentation and became the highest level at 18.072 ㎎/g at the 60 hours of it. In accordance with the fermentation of Chungkook-Jang, pH got to the 8.39 at 60 hours with increasing, protease activity was increased according to the fermentation and acid and neutral protease activity was reduced after being reached at the highest activity at 48 hours. The most suitable pH was 6.5 and temperature was 35℃ for dissolution-activated of protein in the process of fermentation of Chungkook-Jang. The content of water soluble protein and the content of salt soluble protein were increased at continuously according to the fermentation time of Chungkook-Jang the largest quantity. The molecular weight of water soluble protein of Chungkook-Jang fermented for 48 hours was about 19,000. The amino acids of water soluble protein just after steaming were totally 16 kinds and proline was amino acid and them was in series by glutamic acid and serine in that ordered. The amino acids salt soluble protein, just after steaming were totally 16 kinds and was the largest quantity phenylalanine, glutamic acid and aspartic acid and aspartic acid in that order.