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Thermostabilization of Pichia stipitis xylitol dehydrogenase by mutation of structural zinc-binding loop

Paper ID Volume ID Publish Year Pages File Format Full-Text
25372 43570 2007 6 PDF Available
Title
Thermostabilization of Pichia stipitis xylitol dehydrogenase by mutation of structural zinc-binding loop
Abstract

Xylitol dehydrogenase from Pichia stipitis (PsXDH) is one of the key enzymes for the bio-ethanol fermentation system from xylose. Previously, we constructed the C4 mutant (S96C/S99C/Y102C) with enhanced thermostability by introduction of structural zinc. In this study, for further improvement of PsXDH thermostability, we constructed the appropriate structural zinc-binding loop by comparison with other polyol dehydrogenase family members. A high thermostability of PsXDH was obtained by subsequent site-directed mutagenesis of the structural zinc-binding loop. The best mutant in this study (C4/F98R/E101F) showed a 10.8 °C higher thermal transition temperature (TCD) and 20.8 °C higher half denaturation temperature (T1/2) compared with wild-type.

Keywords
XDH, xylitol dehydrogenase; PsXDH, XDH from Pichia stipitis; MDR, medium-chain dehydrogenase/reductase; PDH, polyol dehydrogenase; SDH, sorbitol dehydrogenase; CD, circular dichroism; T1/2, half denaturation temperature; TCD, thermal transition temperatur
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Thermostabilization of Pichia stipitis xylitol dehydrogenase by mutation of structural zinc-binding loop
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 129, Issue 4, 10 May 2007, Pages 717–722
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
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Any Questions? feel free to contact us