Abstract
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.
Original language | English |
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Pages (from-to) | 503-506 |
Number of pages | 4 |
Journal | Applied Microbiology and Biotechnology |
Volume | 36 |
Issue number | 4 |
DOIs | |
Publication status | Published - Jan 1992 |
Externally published | Yes |