中文摘要：

从一个软体动物的全身的 EGXA 酶， Ampullaria crossean，被克隆进 pFastBac 向量然后不同类地在昆虫 Tn5 房间表示了。它的自然 N 终端信号肽在昆虫 Tn5 房间工作了很好。recombinant EGXA 是 63 kDa 蛋白质并且有活跃 endo-β-1,4-glucanase (EC 3.2.1.4 ) 和 e ndo-β-1,4-xylanase (EC 3.2.1.8 ) 。endo-β-1 的 sp ecific 活动， 4-xyla nase 比在 EGX 高，它从 Ampullaria 的纸巾交叉在的胃被净化。EGXA 的 N 终端纤维素绑定领域让它更高效地绑在纤维素和木聚糖。这个纤维素绑定领域也增加了这 recombinant 酶的热稳定性并且减少 recombinant EGXA p-nitrophenyl-β-D-cellobioside 和钠 carboxymethyl 纤维素上的特定的活动。

英文摘要：

A full-length EGXA enzyme from a mollusk, Ampullaria crossean, was cloned into pFastBac vector and then heterogeneously expressed in insect Tn5 cells. Its natural N-terminal signal peptide worked well in the insect Tn5 cells. The recombinant EGXA was a 63 kDa protein and had active endo-β-1,4-glucanase （EC 3.2.1.4） and endo-β-1,4-xylanase （EC 3.2.1.8）. The specific activity of endo-β-1,4-xylanase was higher than in the EGX, which was purified from the stomach tissues of Ampullaria crossen. The N-terminal cellulose-binding domain of EGXA made it bind to cellulose and xylan more efficiently. This cellulose-binding domain also increased the thermal stability of this recombinant enzyme and decreased the recombinant EGXA＇s specific activities on β-nitrophenyl-β-D-cellobioside and sodium carboxymethyl cellulose.