AI Article Synopsis
- A carbohydrate-binding module (CBM2b) from Streptomyces thermoviolaceus was fused with a thermostable xylanase (XynB) from Thermotoga maritima to create a new enzyme called XynB-CBM2b.
- The chimeric enzyme was purified and showed stability at high temperatures (up to 90 degrees C) and a similar pH-activity profile to XynB.
- XynB-CBM2b was effective in binding to insoluble xylan sources and demonstrated slightly improved activity against soluble xylan compared to the original XynB enzyme.
Article Abstract
A family 2b carbohydrate-binding module from Streptomyces thermoviolaceus STX-II was fused at the carboxyl-terminus of XynB, a thermostable and single domain family 10 xylanase from Thermotoga maritima, to create a chimeric xylanase. The chimeric enzyme (XynB-CBM2b) was purified and characterized. It displayed a pH-activity profile similar to that of XynB and was stable up to 90 degrees C. XynB-CBM2b bound to insoluble birchwood and oatspelt xylan. Whereas its hydrolytic activities toward insoluble xylan and p-nitrophenyl-beta-xylopyranoside were similar to those of XynB, its activity toward soluble xylan was moderately higher than that of XynB.
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| http://dx.doi.org/10.1016/s0014-5793(03)00803-2 | DOI Listing |
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