Stabilization of xylanase by random mutagenesis

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 st...

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Veröffentlicht in:	FEBS letters 1993-01, Vol.316 (2), p.123-127
Hauptverfasser:	Arase, Akemi, Yomo, Tetsuya, Urabe, Itaru, Hata, Yasuo, Katsube, Yukiteru, Okada, Hirosuke
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacillus pumilus Biological and medical sciences Endo-1,4-beta Xylanases Enzyme Stability Enzyme stabilization Fundamental and applied biological sciences. Psychology Glycoside Hydrolases - antagonists & inhibitors Glycoside Hydrolases - chemistry Glycoside Hydrolases - genetics Glycoside Hydrolases - metabolism Heat-resistant mutant Hot Temperature Molecular and cellular biology Molecular genetics Mutagenesis Mutagenesis. Repair Protein Structure, Tertiary Random Allocation Random mutagenesis Thermodynamics Xylanase
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Beschreibung
Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(93)81199-A