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- W2019621708 startingPage "1341" @default.
- W2019621708 abstract "Paenibacillus sp. DG-22로부터 세포내 효소인 <TEX>${beta}-xylosidase$</TEX>가 이온교환, 소수성 상호작용, 겔여과 크래마토그래피에 의해 순수하게 정제되었다. 이 효소의 분자량은 겔여과에 의해서는 156,000으로, SDS-PACE에 의해서는 80,000으로 측정되었는데 이것은 이 효소가 동일한 두 소단위로 구성되어 있음을 나타낸다. 정제된 효소는 <TEX>$65^{circ}C$</TEX>와 pH 5.5에서 최대 활성을 나타내었다. 이 효소는 <TEX>$60^{circ}C$</TEX>에서 60분까지 초기 활성의 80%를 유지하였고 <TEX>$65^{circ}C$</TEX>에서 25분의 반감기를 가지고 있었다. 이 효소는 기질로서 pNPX에 매우 특이적이었고 다른 p-nitrophenyl 글리코시드들과 자일란에는 활성을 나타내지 않았다. pNPX에 대한 <TEX>$K_m$</TEX>과 <TEX>$V_{max}$</TEX>는 각각 0.53 mM과 3.18 U/mg단백질이었다. 이 <TEX>${beta}-xylosidase$</TEX>는 <TEX>$Ag^+,;Fe^{2+},;Hg^{2+}$</TEX> 및 <TEX>$Zn^{2+}$</TEX>에 의해 강하게 억제되었으며 DTT에 의해서 약간 활성화되었다. 자일로바이오스, 자일로트라이오스 및 자일로데트라오스로부터의 가수분해 산물은 자일로오스이었다. An intracellular <TEX>${beta}-xylosidase$</TEX> from Paenibacillus sp. DG-22 was purified to homogeneity by ion-exchange, hydrophobic interaction and gel-filtration chromatography. The molecular weight of the enzyme was measured to be 156,000 by gel filtration and 80,000 by SDS-PAGE, indicating that the enzyme consisted of two identical subunits. The purified enzyme exhibited maximum activity at <TEX>$65^{circ}C$</TEX> and pH 5.5. It retained 89% of its initial activity up to 60 min at <TEX>$60^{circ}C$</TEX> and had a half-life of 25 min at <TEX>$65^{circ}C$</TEX>. The enzyme was highly specific for pNPX as the substrate. It showed little or no activity against other p-nitrophenyl glycosides and xylans. The <TEX>$K_m;and;V_{max}$</TEX> for pNPX was 0.53 mM and 3.18 U/mg protein, respectively. The <TEX>${beta}-xylosidase$</TEX> was strongly inhibited by <TEX>$Ag^+,;Fe^{2+},;Hg^{2+};and;Zn^{2+}$</TEX> and slightly activated by DTT. The hydrolysis product from xylobiose, xylotriose, and xylotetraose was xylose." @default.
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- W2019621708 date "2007-10-30" @default.
- W2019621708 modified "2023-09-25" @default.
- W2019621708 title "Purification and Characterization of β-Xylosidase from Paenibacillus sp. DG-22" @default.
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- W2019621708 doi "https://doi.org/10.5352/jls.2007.17.10.1341" @default.
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