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Cellulomonas sp . ATCC 21399에서 Cellulase 분리 및 그 특성
한동표,김택영 ( Dong Pyou Han,Taik Yung Kim ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.3
Cellulomonas sp. ATCC 21399 contained at least 9 components with carboxylmethyl cellulase (CMCase) activity determined by non-denaturing polyacrylamide gel electrophoresis (PAGE). One of the active components was purified through ammonium sulfate fractionation, Sephadex G-150 gel filtration chromatography, and DEAE-Sephadex A-25 ion exchange chromatography. The degree of purification of the enzyme was determined by PAGE and SDS-PAGE. The enzyme was glycosylated, and its molecular weight was estimated to be about 64,000 in SDS-PAGE. The optimum temperature for the enzyme was about 55℃. The enzyme activity was optimum at pH 5.5, and was constant from pH 7.0 to 8.5. Thermalstability studies showed that the enzyme was completely inactivated after 2×(1/2) hour incubation at 60℃, and 4 hour incubation at 55℃. But the enzyme was stable after 6 hour incubation at 50℃.
Isolation and Characterization of a Cellulase from Cellulomonas sp. ATCC 21399
한동표,김택영,Han, Dong-Pyou,Kim, Taik-Yung 생화학분자생물학회 1987 한국생화학회지 Vol.20 No.3
Cellulomonas sp. ATCC 21399는 carboxymethyl cellulase (CMCase) activity를 가지는 성분을 분비하는데 이 cellulase activity는 nondenaturing polyacrylamide gel electrophoresis (PAGE) 법과 CMC agar replica 법을 이용, 측정하여 9가지의 성분으로 분리 확인되었다. 이들 중 한 성분을 ammonium sulfate 분획분리, Sephadex G-150 gel filtration 크로마토그라피, DEAE-Sephadex A-25 이온교환 크로마토그라피 방법 등으로 분리 정제하였다. 효소의 정제 정도는 PAGE와 SDS-PAGE 방법을 이용하여 확인하였다. 이 효소는 당단백질이며 분자량이 약 64,000으로 추정되었다. 이 효소의 활성도가 최적인 온도는 $55^{\circ}C$이고, 최적 pH는 5.5로 밝혀졌고 pH 7.0에서 8.5 사이에는 활성도에 변화는 주지 않음이 밝혀졌다. 열 안정성 조사에서 이 효소률 $60^{\circ}C$에서 $2\frac{1}{2}$ 시간동안 열처리 시키면 활성도를 완전히 상설하지만 $55^{\circ}C$에서는 4시간동안 열처리 시켜야 활성도가 완전히 사라졌다. 그러나 $50^{\circ}C$에서 6시간동안열처리에서도 매우 안정했다. Cellulomonas sp. ATCC 21399 contained at least 9 components with carboxylmethyl cellulase (CMCase) activity determined by non-denaturing polyacrylamide gel electrophoresis (PAGE). One of the active components was purified through ammonium sulfate fractionation, Sephadex G-150 gel filtration chromatography, and DEAE-Sephadex A-25 ion exchange chromatography. The degree of purification of the enzyme was determined by PAGE and SDS-PAGE. The enzyme was glycosylated, and its molecular weight was estimated to be about 64,000 in SDS-PAGE. The optimum temperature for the enzyme was about $55^{\circ}C$. The enzyme activity was optimum at pH 5.5, and was constant from pH 7.0 to 8.5. Thermalstability studies showed that the enzyme was completely inactivated after $2\frac{1}{2}$ hour incubation at $60^{\circ}C$, and 4 hour incubation at $55^{\circ}C$. But the enzyme was stable after 6 hour incubation at $50^{\circ}C$.