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Purification and Properties of Two Thermostable Alkaline Xylanases from an Alkaliphilic Bacillus sp.

机译:两种嗜碱芽孢杆菌的热稳定性碱性木聚糖酶的纯化和性质。

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摘要

Two xylanases, designated XylA and XylB, were purified from the culture supernatant of the alkaliphilic Bacillus sp. strain AR-009. The molecular masses of the two enzymes were estimated to be 23 kDa (XylA) and 48 kDa (XylB) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimum pHs for activity were 9 for XylA and 9 to 10 for XylB. The temperature optima for the activity of XylA were 60°C at pH 9 and 70°C at pH 8. XylB was optimally active at 75°C at pH 9 and 70°C at pH 8. Both enzymes were stable in a broad pH range and showed good stability when incubated at 60 and 65°C in pH 8 and 9 buffers.
机译:从嗜碱芽孢杆菌属菌种的培养上清液中纯化出两种木聚糖酶,分别命名为XylA和XylB。菌株AR-009。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳估计这两种酶的分子量分别为23 kDa(XylA)和48 kDa(XylB)。活性的最佳pH对于XylA为9,对于XylB为9至10。 XylA活性的最适温度是pH值为9的60°C和pH值为8的70°C。XylB的最佳活性是75°C的pH值为9和70°C的pH为8。两种酶在宽pH下均稳定在60和65°C下在pH 8和9的缓冲液中孵育时显示出良好的稳定性。

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