In vitro mutagenesis of a xylanase from the extreme thermophile Caldocellum saccharolyticum.
Six mutant xylanases were obtained by in vitro mutagenesis of a xylanase gene from the extremely thermophilic bacterium Caldocellum saccharolyticum. The temperature stability of all enzymes was affected by mutation to various degrees and one of the xylanases had an altered temperature optimum. The mutations had no effect on the pH optimum. The C. saccharolyticum xylanase showed strong homology to several thermophilic and mesophilic xylanases, and comparison of primary sequences allowed the localization of probable active sites and residues involved in thermostability.
Department of Cellular and Molecular Biology, University of Auckland, New Zealand.
E
E
Lüthi
K
K
Reif
N B
NB
Jasmat
P L
PL
Bergquist
D000595:Amino Acid Sequence; D001421:Bacteria, Anaerobic / Q000235:genetics*; D004795:Enzyme Stability / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D006026:Glycoside Hydrolases / Q000235:genetics*; D006358:Hot Temperature; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009154:Mutation / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D043325:Xylan Endo-1,3-beta-Xylosidase
D006026:Glycoside Hydrolases; D043325:Xylan Endo-1,3-beta-Xylosidase