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Acinetobacter sp . stranin JCI DSM 3803 에서 분리된 두 가지 세포내 단백질 가수 분해효소의 특성
김응빈,김영민 ( Eung Bin Kim,Young Min Kim ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.3
Two proteases, protease I and II, from cells of Acinetobacter sp. strain JC1 grown on nutrient broth were purified to better than 95% homogeneity in five steps using azocoll as a substrate. The final specific activities of protease I and II were 107 and 2,889 ㎍ of azocoll hydrolyzed per min per mg of protein, respectively. Protease II contributed to about 95% of the total protease activity. The molecular weights of the native enzymes of protease I and II were determined to be 55,000 ad 44,000, respectively. Sodium dodecyl sulfate-gel electrophoresis revealed the two enzymes to be monomers. The enzymes were found to be serinetype proteases, and were present only in cells grown in complex medium. The activity of protease I was stimulated significantly by Ca^(2+) and Mg^(2+), but that of protease II was not. The enzymes were inhibited completely by Hg^(2+), Zn^(2+), Cu^(2+), Fe^(2+) and EDTA. EGTA showed no inhibitory effect on the two enzymes. The EDTA-inhibited protease II was reactivated by Ca^(2+), Mg^(2+), Mn^(2+), and Co^(2+). Maximal reaction rate of protease I was observed at pH 8.0 and 50℃, and that of protease II was found at pH 8.0 and 60℃. The isoelectric points of protease I and II were found to be 6.9 and 7.1, respectively. Azocasein and casein were hydrolyzed by both enzymes, but bovine serum albumin and carbon monoxide dehydrogenase were not.
Acinetobacter sp. strain JC1 DSM 3803에서 분리 정제된 두 가지 세포내 단백질 가수 분해효소의 특성
김응빈,김영민,Kim, Eung-Bin,Kim, Young-Min Korean Society for Biochemistry and Molecular Biol 1990 한국생화학회지 Vol.23 No.3
Nutrient broth에서 성장한 Acinetobacter sp. strain JC1으로부터 azocoll을 기질로 사용하여 95%이상의 순도를 지닌 두 가지 단백질 가수분해효소(protease I과 II)를 분리, 정제하였다. 두 효소의 최종 specific activity는 protease II가 protease I보다 약 27배 높았으며, 분자량은 protease I이 55,000이고 protease II가 44,000인 것으로 밝혀졌고, 두 효소 모두 한 개의 소단위로 구성되어 있음이 확인되었다. 정제된 두 효소는 serine-type의 단백질 가수분해효소로 minimal medium에서 성장한 세균에서는 형성되지 않았다. Protease I의 활성은 $Ca^{2+}$에 의해 증가되었으나 protease II는 영향을 받지 않았다. 두 효소는 모두 $Hg^{2+}$, $Zn^{2+}$, $Cu^{2+}$, $Fe^{2+}$, EDTA에 의해 활성이 완전히 억제되었으나 EGTA에 의해서는 영향을 받지 않았고, EDTA에 의해 억제된 protease II는 $Ca^{2+}$, $Mg^{2+}$, $Mn^{2+}$, $Co^{2+}$에 의해 활성이 회복되었다. Protease I은 pH8.0과 $50^{\circ}C$에서, protease II는 pH8.0과 $60^{\circ}C$에서 가장 높은 활성을 나타내었다. Protease I의 pI는 6.9, protease II의 pI는 7.1로 측정되었으며, 두 효소 모두 azocoll외에 azocasein과 casein도 가수분해하였으나 bovine serum albumin과 일산화탄소 산화효소는 가수분해하지 못하였다. Two proteases, protease I and II, from cells of Acinetobacter sp. strain JC1 grown on nutrient broth were purified to better than 95% homogeneity in five steps using azocoll as a substrate. The final specific activities of protease I and II were 107 and $2,889{\mu}g$ of azocoll hydrolyzed per min per mg of protein, respectively. Protease II contributed to about 95% of the total protease activity. The molecular weights of the native enzymes of protease I and II were determined to be 55,000 ad 44,000, respectively. Sodium dodecyl sulfate-gel electrophoresis revealed the two enzymes to be monomers. The enzymes were found to be serinetype proteases, and were present only in cells grown in complex medium. The activity of protease I was stimulated significantly by $Ca^{2+}$ and $Mg^{2+}$, but that of protease II was not. The enzymes were inhibited completely by $Hg^{2+}$, $Zn^{2+}$, $Cu^{2+}$, $Fe^{2+}$ and EDTA. EGTA showed no inhibitory effect on the two enzymes. The EDTA-inhibited protease II was reactivated by $Ca^{2+}$, $Mg^{2+}$, $Mn^{2+}$, and $Co^{2+}$. Maximal reaction rate of protease I was observed at pH 8.0 and $50^{\circ}C$, and that of protease II was found at pH 8.0 and $60^{\circ}C$. The isoelectric points of protease I and II were found to be 6.9 and 7.1, respectively. Azocasein and casein were hydrolyzed by both enzymes, but bovine serum albumin and carbon monoxide dehydrogenase were not.
Depolymerization and decomplexation of soil humic acids by an Antarctic Pseudomonas strain
김덕규,윤의중,김응빈,이형석 한국미생물학회 2023 미생물학회지 Vol.59 No.4
With recent rapid warming in the maritime Antarctic, the susceptibility of soil organic matter to microbial decomposition is an emerging topic related to CO2 emission and vegetation changes. Soil humic acids (HA) enter the Antarctic ecosystems as small-soluble organic compounds resulting from microbial decomposition. Antarctic and commercial HAs were incubated with Antarctic Pseudomonas sp. PAMC 29040 with an esterase activity and structural changes in the resulting HA samples were then investigated. Gel permeation chromatography revealed the depolymerization of the large molecular fractions of both Antarctic and commercial HAs. Solid-state 13C-nuclear magnetic resonance spectroscopy showed an increase in the aromaticity degree which can be attributed to the increased intensity of aromatic-C signals upon the cleavage of interior C–C and C–O –C linkages (e.g., decomplexation by esterase activity), while the Fourier-transform infrared spectroscopy did not provide any information on the changes in the functional groups, such as Ar–OH and Ar–COOH, or bonding patterns in the HAs. To the best of our knowledge, this is the first report showing direct evidence of HA decomposition capacity by soil bacteria in an Antarctic terrestrial ecosystem.