The effects of glycerol polyethylene glycol fructose glucose sorbitol and saccharose on the conformation and catalytic activity of α-chymotrypsin were studied in 0.1 M sodium phosphate buffer and buffered aqueous 60% ethanol (pH 8.0). The enzyme activity was practically completely lost within 10 min in 60% ethanol but in the presence of stabilizers the activity was retained. With the exception of polyethylene glycol the stabilizing effect decreased with increase of the incubation time. The preservation of the catalytic activity was accompanied by changes in the secondary and tertiary structures of α-chymotrypsin.
|Number of pages||5|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - Jan 1 2002|
- Enzyme structure
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology