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. 1993 Jan 25;316(2):123-7.
doi: 10.1016/0014-5793(93)81199-a.

Stabilization of xylanase by random mutagenesis

A Arase  1 , T Yomo, I Urabe, Y Hata, Y Katsube, H Okada
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Free article

Stabilization of xylanase by random mutagenesis

A Arase et al. FEBS Lett. .
Free article

Abstract

Four heat-resistant mutants of xylanase (N56, N102, N104 and F1) were obtained by random mutagenesis. The mutant genes had the following amino acid changes: N56, Ser-26 to Trp, Gly-38 to Asp and Thr-126 to Ser; N102, Gly-38 to Asp; N104, Gly-38 to Ser and Arg-48 to Lys; F1, Ser-12 to Cys. Kinetic studies showed that N104 is stabilized by an increase in the activation enthalpy, while the other mutants are stabilized by a decrease in the activation entropy.

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