M. Iwakura et al., An approach for protein to be completely reversible to thermal denaturation even at autoclave temperatures, PROTEIN ENG, 14(8), 2001, pp. 583-589
Reversibility of protein denaturation is a prerequisite for all application
s that depend on reliable enzyme catalysis, particularly, for using steam t
o sterilize enzyme reactors or enzyme sensor tips, and for developing prote
in-based devices that perform on-off switching of the protein function such
as enzymatic activity, ligand binding and so on. In this study, we have su
ccessfully constructed an immobilized protein that retains full enzymatic a
ctivity even after thermal treatments as high as 120 degreesC. The key for
the complete reversibility was the development of a new reaction that allow
ed a protein to be covalently attached to a surface through its C-terminus
and the protein engineering approach that was used to make the protein comp
atible with the new attachment chemistry.