An approach for protein to be completely reversible to thermal denaturation even at autoclave temperatures

Citation
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
Citations number
38
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEIN ENGINEERING
ISSN journal
0269-2139 → ACNP
Volume
14
Issue
8
Year of publication
2001
Pages
583 - 589
Database
ISI
SICI code
0269-2139(200108)14:8<583:AAFPTB>2.0.ZU;2-T
Abstract
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.