Picture of wind turbine against blue sky

Open Access research with a real impact...

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

The Energy Systems Research Unit (ESRU) within Strathclyde's Department of Mechanical and Aerospace Engineering is producing Open Access research that can help society deploy and optimise renewable energy systems, such as wind turbine technology.

Explore wind turbine research in Strathprints

Explore all of Strathclyde's Open Access research content

Chemical modification causes similar change in dependence on water activity of chymotrypsin hydration and catalysis in hexane

Rees, D.G. and Gerashchenko, ll. and Kudryashova, E.V. and Mozhaev, V.V. and Halling, P.J. (2002) Chemical modification causes similar change in dependence on water activity of chymotrypsin hydration and catalysis in hexane. Biocatalysis and Biotransformation, 20 (3). pp. 161-166. ISSN 1024-2422

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

Abstract

Amino groups in alpha-chymotrypsin were reacted with pyromellitic anhydride, introducing 17 to 32 additional carboxyl groups. This modification causes a major change in the water adsorption isotherm of the lyophilized protein powder. Little water is bound by the modified enzyme at water activity (a(w)) below 0.35, but it shows increased water binding at a(w) over 0.5. This correlates with a similar change in the a(w) dependence of the catalytic activity of the enzyme powder suspended in hexane, with a much steeper increase in activity of the modified chymotrypsin.