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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

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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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