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김석환,김석지,김기남,박인식 東亞大學校附設遺傳工學硏究所 1997 遺傳工學硏究 Vol.- No.4
파로부터 acid phosphatase를 Sepharcyl S-200 gel filtration과 CM-Sepharose CL-6B ion exchange chromatography 를 이용하여 부분정제하였다. p-Ni-trophenyl phosphate를 기질로 사용했을 경우에 최적pH는 5.5, 최적온도는 60℃였다. 효소의 활성화 에너지는 4.86kcal/mole이었다. 효소는 pH6.0에서 가장 안정하였으며, 50℃이하에서 대체로 안정하였다. 효소는 p-nitrophenyl phosphate를 기질로 가장 잘 이용하였으며, 5'-IMP와 5'-GMP는 기질로 거의 이용하지 못하였다. 효소는 p-nitrophenyl phosphate를 기질로 했을 경우에 ??값이 0.87mM이었다. Cr+++, Zn++, Cu++ 이온은 효소의 활성을 저해하였으며, 또한 molybdate와 metavandate 이온이 효소의 활성을 저해하였다. 그리고, NaCl의 농도가 높을수록 효소의 활성을 저해하였다. Acid phosphatase (EC 3.1.3.2) from welsh onion was partially purified by Sephacryl S-200 gel filtration and CM-Sepharose CL-6B ion exchange chromatography. The optimum pH and temperature of acid phosphatase from green onion were pH 5.5 and 60℃, respectively. The enzyme was the most stable at pH 6.0 and unstable above pH 9.0. The activation energy of the enzyme was determined to be 4.86 kcaL/mole. The enzyme utilized p-nitrophenyl phosphate most as a best substrate among tested possible substrates, while 5'-GMP and 5'-IMP were poor substrates for the enzyme. ?? of the enzyme with p-nitrophenyl phosphate as a substrate was identified as 0.87 mM. Among metal ions and inhibitors tested, Cr+++, Zn++, Cu++, molybdate and metavanadate ions inhibited the enzyme reaction drastically.
Characterization of Acid Phosphatase from Carrots
Kim, Gi-Nahm The Korean Society of Food Science and Nutrition 1994 한국식품영양과학회지 Vol.23 No.3
Acid phosphatase (EC3.1.3.2) from carrots was partially purified by ammonium sulfate fractionation (30%-80%), Sephacryl S-200 gel filtration, cm-Sepharose CL-6B and DEAE -Sephacel ion exchange chromatography. The optimum ph and temperature of acid phosphatase from carrots were pH 5.5 and 55$^{\circ}C$, respectively. The enzyme was most stable at ph 6.0 and relatively unstable below pH 4.0 . The activation energy of the enayme was determined to be 10.6kcal/mole. The enzyme utilized p-nitrophenyl phosphate as a substrate among tested possible substrates, whereas it hydrolyzed 5' -IMP and 5'-GMP poorly. The Michaelis -Menten constant(Km) of the enzyme with p-nitrophenyl phosphate as a substrate was identified as 0.55mM. Amongtested metal ions and inhibitors, Al+++ Zn++, Cu++ , fluoride, metavanadate and molybdate ions inhibited the enzyme activity drastically.
Characterization of Acidic Nucleotidase from Aspergillus niger
Kim, Gi Nahm,Park, In Shik 한국산업미생물학회 1992 한국미생물·생명공학회지 Vol.20 No.1
Aspergillus niger로부터 acidic nucleotidase를 Sepharose CL-6B gel 여과와 DEAE-Sephacel 이온교환수지를 이용하여 부분정제하였다. 5'-AMP와 3'-AMP를 기질로 사용했을 경우에 효소의 최적 pH는 4.5, 그리고 최적온도는 55℃였다. 그러나, p-nitro-phenyl phosphate를 기질로 사용했을 경우에는 최적 pH는 변화가 없었으나, 최적온도는 70℃였다. 효소의 활성화에너지는 3'-AMP, 5'-AMP 그리고 p-nitrophenyl phosphate를 기질로 사용했을 경우에 각각 4.76kcal/mole, 6.95kcal/mole 그리고 11.82kcal/mole였다. 본 효소는 산성 pH에서 안정하였다. 효소의 활성은 nucleotide, nucleoside 및 무기 인산을 첨가하였을 경우에 변화가 거의 없었다. Ferric, aluminium, vanadate 그리고 molybdate 이온은 효소의 활성을 저해하였다. 효소는 3'-AMP, 5'-AMP 및 p-nitrophenyl phosphate에 대해서 K_m값이 각각 1.39mM, 1.5mM 및 5.77mM였다. 본 효소의 substrate efficiency(V_max/K_m)는 3'-AMP가 가장 높았다. Acidic nucleotidase from Aspergillus niger has been partially purified by Sepharose CL-6B gel filtration and DEAE-Sephacel ion exchange chromatography. The optimum pH and temperature for the enzyme reaction with 5'-AMP or 3'-AMP as a substrate were 4.5 and 55℃, respectively. However, the optimum temperature became 70℃ when p-nitrophenyl phosphate was used as a substrate. The enzyme was stable at acidic pH. The enzyme activity was not affected by addition of various nucleotides, nucleosides and inorganic phosphates. Ferric, aluminium, vanadate and molybdate ions inhibited the enzyme activity dramatically. In kinetic studies, K_m values for 3'-AMP, 5'-AMP and p-nitrophenyl phosphate were 1.39mM, 1.5mM and 5.77mM, respectively. The substrate efficiency (V_max/K_m) shows 3'-AMP is the prefered substrate for the enzyme among tested substrates.
Kim,Gi-Nahm,Kil,Ji-Oeun,Park,Inshik 東亞大學校附設遺傳工學硏究所 1996 遺傳工學硏究 Vol.- No.3
β-1,3-Glucanase from Bacillus sp. isolated from the soil has been partially purified by ethanol precipitation, Sephacryl S-200 gel filtration and DEAE-Sephacel ion-exchange chromatography. The optimum pH and temperature for the enzyme reaction with laminarin as a substrate were found to be pH 4.5 AND 55℃, respectively. The enzyme was most stable at pH range between 4.0 and 7.0. It was inactivated completely within 10 min at 55℃, but thermostability of the enzyme could be increased by the addition of CaCl₂. The Michaelis-Menten constant of the enzyme with laminarin was 4.76 mg/ml. The enzyme was inhibited by metal ions such as Hg²+, Fe³+ and Cu²+. N-Bromosuccinimide inhibited the enzyme activity completely at 10 mM, whereas sulfhydryl reagents increased the enzyme activity.
Characterization of Acid Phosphatase from Carrots
김기남(Gi-Nahm Kim),신미해(Mi-Hae Shin),박인식(Inshik Park) 한국식품영양과학회 1994 한국식품영양과학회지 Vol.23 No.3
당근으로부터 acid phosphatase를 유안염석 (30%~80%), Sephacryl S-200gel 여과, CM-Sepharose CL-6B양이온 교환수지, 그리고 DEAE-Sephacel 음이온 교환수지를 이용하여 부분정제하였다. p-nitrophenyl phosphate를 기질로 사용했을 경우에 최적 pH는 5.5, 그리고 최적온도는 55℃였다. 효소의 활성화에너지는 10.3㎉/㏖e였다. 효소는 pH 6.0에서 가장 안정하였으며, 50℃하에서 대체로 안정하였다. 효소는 p-nitrophenyl phosphate를 기질로 가장 잘 이용하였으며, 5'-IMP 와 5' -GMP는 기질로 거의 이용하지 못하였다. 효소는 p-nitrophenyl phosphate를 기질로 했을 경우에 K_m값이 0.55mM 이었다. Aluminium, zinc, mercury 이온은 효소의 활성을 저해하였으며, 또한 fluoride, metavanadate, molybdate 이온과 L-phenylalanme도 효소의 활성을 저해하였다. Acid phosphatase(EC 3.1.3.2) from carrots was partially purified by ammonium sulfate fractionation(30%~80%), Sephacryl S-200 gel filtration, CM-Sepharose CL-6B and DEAE-Sephacel ion exchange chromatography. The optimum pH and temperature of acid phosphatase from carrots were pH 5.5 and 55℃, respectively. The enzyme was most stable at pH 6.0 and relatively unstable below pH 4.0. The activation energy of the enzyme was determined to be 10.6㎉/㏖e. The enzyme utilized p-nitrophenyl phosphate as a substrate among tested possible substrates, whereas it hydrolyzed 5'-IMP and 5'-GMP poorly. The Michaelis-Menten constant(Km) of the enzyme with p-nitrophenyl phosphate as a substrate was identified as 0.55mM. Among tested metal ions and inhibitors, AI^(+++), Zn^(++), Cu^(++), fluoride, metavanadate and molybdate ions inhibited the enzyme activity drastically.