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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.
Serratia liquefaciens AL-11이 생산하는 Alkaline Lipase의 특성 및 작용양상
최청,김태완,안봉전,김영활,손준호,김성,최희준 한국미생물생명공학회 ( 구 한국산업미생물학회 ) 1996 한국미생물·생명공학회지 Vol.24 No.1
본 효소의 최적 반응온도는 약 45℃이고, 최적 pH는 10.0 정도였고, pH 7.0~10.0 범위와 30~50℃의 범위에서 안정하였다. 금속이온중 Mn^2+, Ca^2+ 등에 의하여 활성이 증대되었으나 Fe^2+, Pb^2+와 Zn^2+ 등에 의해서는 효소 활성이 저해되었고, 효소활성 저해제 중 ethylenediaminetetraacetic acid(EDTA)에 의해 강한 저해작용을 나타내어 본 효소는 효소분자 중 금속이온이 관여하는 것으로 추정되었다. 효소반응 처리한 olive oil 가수분해물을 박충크로마토그래피 분석한 결과 Serratia liquefaciens AL-11이 생산하는 지방분해효소는 기질특이성이 비특이적이었으며, sodium cholate, sodium edoxychol-ate, sodium taurocholate 등의 담즙산염에 의해 효소활성이 증대되었다. The optimum temperature and pH for the enzyme activity were 45℃ and 10.0, respectively. The enzyme was stable in a pH range of 5 to 10, and 62% of its activity was lost on heat treatment at 60℃ for 20 min. The activity of the purified enzyme was inhibited by Fe^2+, Zm^2+ and Pb^2+, and slightly activated by Mn^2+ and Ca^2+. γ-Chloromercuribenzoic acid, 2,4-dinitrophenol and H_2O_2 did not show inhibitory effect on the lipolytic activity of the alkaline lipase but ethylenediaminetetraacetic acid inhibited the enzyme activity. This suggested that the enzyme have metal group in its active site. Sodium salts of bile acids stimulated the enzyme activity. Analysis of hydrolyzates of olive oil after the lipase reaction revealed that Serratia liquefaciens AL-11 produced non-specific lipolytic enzyme.