Molecular Properties and Enhancement of Thermostability by Random Mutagenesis of Glutamate Dehydrogenase from Bacillus subtilis.

Autor: Khan, Md. Iqbal Hassan, Ito, Kousuke, Hyeung Kim, Hiroyuki Ashida, Ishikawa, Takahiro, Shibata, Hitoshi, Sawa, Yoshihiro
Předmět:
Zdroj: Bioscience, Biotechnology & Biochemistry; Oct2005, Vol. 69 Issue 10, p1861-1870, 10p, 2 Diagrams, 3 Charts, 7 Graphs
Abstrakt: The article examines the molecular properties and enhancement of the thermostability of glutamate dehydrogenase from Bacillus subtilis by random mutagenesis. An error-prone polymerase chain reaction was performed to improve the stability of the enzyme. Two single mutant enzymes, Q144R and E27F were isolated from the final mutant library. It has been discovered that Q144 can be used as a template gene to modify the substrate specificity of Bs-GluDH for industrial use.
Databáze: Supplemental Index