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 Unfolding of cardosin A in organic solvents and detection of intermediaries
Please use this identifier to cite or link to this item http://hdl.handle.net/10773/6785

title: Unfolding of cardosin A in organic solvents and detection of intermediaries
authors: Sarmento, Ana Cristina
Oliveira, Cláudia S.
Pereira, Anabela
Esteves, Valdemar I.
Moir, Arthur J.G. Moir
Saraiva, Jorge
Pires, Euclides
Barros, Marlene
keywords: Aspartic proteinases
Organic solvents
issue date: 2009
publisher: Elsevier
abstract: In the present study the relationship between conformational stability and enzymatic activity in the presence of organic solvents (OS) was investigated. We have found that cardosin A, the model protease investigated in this work, inactivates through a biphasic mechanism, which is incipient in aqueous buffer and becomes visible in the presence of hydrophilic OS. In fact, in OS this inactivation originates stable intermediaries thatwere detected in acetonitrile. This biphasic mechanism can be described in two phases: an initial one, where OS induce alterations that affect the active site cleft and global mobility, but with little interference on the global protein conformation, and, a second phase, where there is a global change in protein conformation with concomitant activity loss. It is shown that in the presence of hydrophilic OS there is a larger mobility of the enzyme, revealed by limited proteolysis, probably due to a weakening of hydrophobic interactions within the protein core.
URI: http://hdl.handle.net/10773/6785
ISSN: 1381-1177
publisher version/DOI: http://dx.doi.org/10.1016/j.molcatb.2008.08.004
source: Journal of Molecular Catalysis B: Enzymatic
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