title: Stabilization of xylanase by random mutagenesis.
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.
authors.affiliation: Department of Biotechnology, Faculty of Engineering, Osaka University, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Arase
authors.forename: T
authors.initials: T
authors.lastname: Yomo
authors.forename: I
authors.initials: I
authors.lastname: Urabe
authors.forename: Y
authors.initials: Y
authors.lastname: Hata
authors.forename: Y
authors.initials: Y
authors.lastname: Katsube
authors.forename: H
authors.initials: H
authors.lastname: Okada
mesh_terms: D043364:Endo-1,4-beta Xylanases; D004795:Enzyme Stability; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature; D016296:Mutagenesis; D017434:Protein Structure, Tertiary; D011897:Random Allocation; D013816:Thermodynamics
chemical_list: D006026:Glycoside Hydrolases; D043364:Endo-1,4-beta Xylanases