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 degrees C higher thermal transition temperature (T(CD)) and 20.8 degrees C higher half denaturation temperature (T(1/2)) compared with wild-type.

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@article{Annaluru2007ThermostabilizationOP, title={Thermostabilization of Pichia stipitis xylitol dehydrogenase by mutation of structural zinc-binding loop.}, author={Narayana Annaluru and Seiya Watanabe and Seung Pil Pack and Ahmed Abu Saleh and Tsutomu Kodaki and Keisuke Makino}, journal={Journal of biotechnology}, year={2007}, volume={129 4}, pages={717-22} }