Picture of virus under microscope

Research under the microscope...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

Explore SIPBS research

Cardosin A as a model aspartic proteinase for the study of organic solvent effects. An overview on catalytic and structural aspects

Sarmento, A.C. and Oliveira, C. and Pires, E. and Halling, P.J. and Barros, M.T. (2003) Cardosin A as a model aspartic proteinase for the study of organic solvent effects. An overview on catalytic and structural aspects. Journal of Molecular Catalysis B: Enzymatic, 21 (1-2). pp. 19-23. ISSN 1381-1177

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

Water has proven to be one of the several limitations for broadening the scope of applications of enzymes in biocatalysis, especially when the reactants involved are poorly water-soluble. The introduction of an organic solvent into the reaction system has numerous advantages. These include a direct action of the solvents on the reactants (improving their solubility) and on the reaction products (improving or diminishing their solubility), thereby increasing the productivity of the reaction system. Nevertheless, it has been documented that the introduction of an organic solvent into the reaction mixture may induce alterations on enzyme activity, enzyme stability and thermostability, and enzyme specificity thereby imprinting new properties to old enzymes.