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Aspergillus nidulans FGSC 159 의 β - Glucosidase 특성 및 효소작용
정재성,하영칠,홍순우 ( Jae Sung Jung,Yung Chil Hah,Soon Woo Hong ) 생화학분자생물학회 1983 BMB Reports Vol.16 No.2
Crude enzyme solution prepared from the culture filtrate of Aspergillus nidulans FGSC 159 in CMC minimal liquid medium was fractionated through a three-step procedure including chromatography on Sephadex G-150, DEAE-Sephadex A-50 and Sephadex G-200. Three β-glucosidase components, P-I-Ia, P-II-Ia and P-II-Ib, were prepared. All the fractions had their highest activities at pH 6.0. Optimum temperatures were 55℃ for P-I-Ia, P-II-Ia and 60℃ for P-II-Ib, respectively. P-II-Ia was a little more thermostable than the other two components. The substrates specificities for these β-glucosidase preparations were investigated. These enzymes showed specificities to cellooligosaccharides and sugar derivatives with β-glucosidic linkage such as cellobiose, cellotriose, cellotetraose, cellopentaose, sophorose, PNPG and salicin. All three fractions not only hydrolyzed substrates to remove glucosyl residues one by one from non-reducing end but also transferred the glucosyl residues to other acceptor molecules. But P-I-Ia showed some different mode of action from the other two fractions. It did not accumulate transglucosylated products in detectable amounts, when reacted with cellooligosaccharides.
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Aspergillus nidulans FGSC 159의 $\beta$-Glucosidase 특성 및 효소작용
정재성,하영칠,홍순우,Jung, Jae-Sung,Hah, Yung-Chil,Hong, Soon-Woo 생화학분자생물학회 1983 한국생화학회지 Vol.16 No.2
Aspergillus nidulans FGSC 159의 cellulase system에 관한 연구의 일환으로, CMC 최소배치에서 배양하여 얻은 crude enzyme을 Sephadex G-150, DEAE-Sephadex A-50, Sephadex G-200의 세 단계의 chromatography과정으로 정제하여 P-I-Ia, P-II-Ia 및 P-II-Ib의 세 가지, $\beta$-glucosidase성분으로 분리하였다. 세 효소성분 모두 pH 6.0정도에서 활성도가 가장 놓았으며 최적온도는 P-I-Ia와 P-II-Ia의 경우는 $55^{\circ}C$, P-II-Ib는 $60^{\circ}C$로 나타났다. 한편 열 안정성은 P-II-Ia는 $55^{\circ}C$까지 유지하다가 급격히 활성을 읽는데 반해 P-II-Ib와 P-I-Ia는 $55^{\circ}C$에서 각각 90%, 60% 정도의 활성을 나타내다가 그 이상의 온도에서 활성을 잃었다. 여러 기질에 대한 작용양상을 HPLC로 분석한 결과 cellobiose, sophorose, cellotriose, cellotetraose, cellopentaose, PNPG, salicin들과 같은 $\beta$-glucoside결합을 하고 있는 화합물에 작용하여 glucose단위로 가수분해 시켰으며 또한 가수분해 단계에서 glucosyl기가 전달되어 transglucosylation이 일어났다. 그러나 P-I-Ia는 cellooligosaccharide와 작용시켰을 때 검출될 수 있을 만큼의 충분한 transglucosylation 생성물이 축적되지 않아 P-I-Ia 및 P-II-Ib와 다른 작용양상을 보였다. Crude enzyme solution prepared from the culture filtrate of Aspergillus nidulans FGSC 159 in CMC minimal liquid medium was fractionated through a three-step procedure including chromatography on Sephadex G-150, DEAE-Sephadex A-50 and Sephadex G-200. Three $\beta$-glucosidase components, P-I-Ia, P-II-Ia and P-II-Ib, were prepared. All the fractions had their highest activities at pH 6.0. Optimum temperatures were $55^{\circ}C$ for P-I-Ia, P-II-Ia and $60^{\circ}C$ for P-II-Ib, respectively. P-II-Ia was a little more thermostable than the other two components. The substrates specificities for these $\beta$-glucosidase preparations were investigated. These enzymes showed specificities to cellooligosaccharides and sugar derivatives with $\beta$-glucosidic linkage such as cellobiose, cellotriose, cellotetraose, cellopentaose, sophorose, PNPG and salicin. All three fractions not only hydrolyzed substrates to remove glucosyl residues one by one from non-reducing end but also transferred the glucosyl residues to other acceptor molecules. But P-I-Ia showed some different mode of action from the other two fractions. It did not accumulate transglucosylated products in detectable amounts, when reacted with cellooligosaccharides.
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