Article
Site-directed saturation mutagenesis at residue F420 and recombination with another beneficial mutation of Ralstonia eutropha polyhydroxyalkanoate synthase.
Biotechnology letters - 1 May 2005
Normi Yahaya M, Hiraishi Tomohiro, Taguchi Seiichi, Sudesh Kumar, Najimudin Nazalan, Doi Yoshiharu
Abstract excerpt
The F420S substitution enhances the specific activity of Ralstonia eutropha PHA synthase (PhaCRe). We have now carried out site-directed saturation mutagenesis of F420 of PhaCRe and, amongst the F420 mutants, the F420S mutant gave the highest poly(3-hydroxybutyrate) (PHB) content. In vitro activity assay showed that the F420S enzyme had a significant decrease in its lag phase compared to that of the wild-type...
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