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- W2040387519 abstract "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-beta-1,4-glucanase (EC 3.2.1.4) and endo-beta-1,4-xylanase (EC 3.2.1.8). The specific activity of endo-beta-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 p-nitrophenyl-beta-D-cellobioside and sodium carboxymethyl cellulose." @default.
- W2040387519 created "2016-06-24" @default.
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- W2040387519 date "2008-11-01" @default.
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- W2040387519 title "The N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates" @default.
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- W2040387519 doi "https://doi.org/10.1111/j.1745-7270.2008.00481.x" @default.
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