1745-7270/asset/ABBS_left.gif?v=1&s=d7c03567db265ca2593d3081e6c1f5eb7fdd879e)
1745-7270/asset/ABBS_right.gif?v=1&s=d6d18fc5d1585069e311beddd193156526022c20)
The N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates
Article first published online: 1 DEC 2008
DOI: 10.1111/j.1745-7270.2008.00481.x
© 2008 Institute of Biochemistry and Cell Biology, SIBS, CAS
Additional Information
How to Cite
Ding, M., Teng, Y., Yin, Q., Zhao, J. and Zhao, F. (2008), The N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates. Acta Biochimica et Biophysica Sinica, 40: 949–954. doi: 10.1111/j.1745-7270.2008.00481.x
Publication History
- Issue published online: 1 DEC 2008
- Article first published online: 1 DEC 2008
- Received: September 08, 2008 Accepted: September 26, 2008
- Abstract
- References
- Cited By
Keywords:
- endo-β-1,4-glucanase;
- endo-β-1,4-xylanase;
- pNPCase;
- CMCase;
- EGXA;
- Ampullaria crossean;
- cellulose-binding domain
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 e ndo-β-1,4-xylanase (EC 3.2.1.8). The sp ecific activity of endo-β-1, 4-xyla nase 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-β-D-cellobioside and sodium carboxymethyl cellulose.