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.
| Item type: | Article |
|---|---|
| ID code: | 309 |
| Notes: | |
| Keywords: | water adsorption, low-water nonpolar media, chymotrypsin, chemical modification, pyromellitic acid, Organic media, alpha-chymotrypsin, enzyme-activity, stability, solvents, protein, esterification, Chemistry |
| Subjects: | Science > Chemistry |
| Department: | Faculty of Science > Pure and Applied Chemistry Unknown Department |
| Related URLs: | |
| Depositing user: | Users 16 not found. |
| Date Deposited: | 13 Mar 2006 |
| Last modified: | 12 Mar 2012 10:35 |
| URI: | http://strathprints.strath.ac.uk/id/eprint/309 |
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