Abstract:
:beta-Glycosidase from the extreme thermophilic archaeon Sulfolobus solfataricus is a tetrameric protein with a molecular mass of 240 kDa, stable in the presence of detergents, and with a maximal activity at temperatures above 95 degrees C. Understanding the structure-activity relationships of the enzyme under different conditions is of fundamental importance for both theoretical and applicative purposes. In this paper we report the effect of methanol, ethanol, 1-propanol, and 1-butanol on the activity of S. solfataricus beta-glycosidase expressed in Escherichia coli. The alcohols stimulated the enzyme activity, with 1-butanol producing its maximum effect at a lower concentration than the other alcohols. The structure of the enzyme was studied in the presence of 1-butanol by circular dichroism, and Fourier-transform infrared and fluorescence spectroscopies. Circular dichroism and steady-state fluorescence measurements revealed that at low temperatures the presence of the alcohol produced no significant changes in the tertiary structure of the enzyme. However, time-resolved fluorescence data showed that the alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
D'Auria S,Nucci R,Rossi M,Bertoli E,Tanfani F,Gryczynski I,Malak H,Lakowicz JRdoi
10.1093/oxfordjournals.jbchem.a022484keywords:
subject
Has Abstractpub_date
1999-09-01 00:00:00pages
545-52issue
3eissn
0021-924Xissn
1756-2651journal_volume
126pub_type
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