Article
Clostridium thermocellum thermostable lichenase with circular permutations and modifications in the N-terminal region retains its activity and thermostability.
Biochimica et biophysica acta - 1 Jan 2015
Tyurin A А, Sadovskaya N S, Nikiforova Kh R, Mustafaev O N, Komakhin R A, Fadeev V S, Goldenkova-Pavlova I V
Abstract excerpt
The Clostridium thermocellum lichenase (endo-β-1,3;1,4-glucan-D-glycosyl hydrolase) displays a high thermostability and specific activity and has a compact protein molecule, which makes it attractive, in particular, for protein engineering. We have utilized in silico analysis to construct circularly permuted (CP) variants and estimated the retained activity and thermostability. New open termini in the region of...
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