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Directed evolution of a mesophilic fungal xylanase by fusion of a thermophilic bacterial carbohydrate-binding module

Paper ID Volume ID Publish Year Pages File Format Full-Text
35404 45088 2011 4 PDF Available
Title
Directed evolution of a mesophilic fungal xylanase by fusion of a thermophilic bacterial carbohydrate-binding module
Abstract

Bacterial GH10 xylanase usually contains carbohydrate-binding module (CBM) that binds to insoluble xylan. Differing from GH10 xylanase, we isolated a fungal GH11 xylanase containing a single catalytic domain from Aspergilus niger (XYN). The thermophilic CBM from Thermotoga maritima (TmCBM9-1_2) might increase the mesophilic XYN's thermo-activity and catalytic efficiency on insoluble xylan, we fused it with the TmCBM9-1_2 behaving as “hand” to grasp xylan actively. The chimeric xylanase XYN-TmCBM9-1_2 exhibited an optimal activity at pH4.2 and 49 °C, 2 °C higher than the thermo-activity of XYN. The chimeric xylanase's activity was 970.1 ± 5.8 U/mg on insoluble oat-spelt xylan, 4.2-fold of that on soluble birchwood xylan (228.1 ± 1.1 U/mg). In contrast, the XYN's activity was 226.9 ± 1.2 U/mg on insoluble oat-spelt xylan, only 40% of that on soluble birchwood xylan (567.2 ± 3.0 U/mg). Fusing with the TmCBM9-1_2 increased the XYN's property, indicating that we can direct to evolve a molecule's function through fusing domains of bacteria and fungi.

Keywords
GH11 xylanase; CBM9; Domain fusion; Thermo-activity; Catalytic efficiency
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Directed evolution of a mesophilic fungal xylanase by fusion of a thermophilic bacterial carbohydrate-binding module
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 46, Issue 1, January 2011, Pages 395–398
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us