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Properties of almond beta-glucosidase immobilized on concanavalin A-sepharose.
- Source :
-
Biochemistry and molecular biology international [Biochem Mol Biol Int] 1993 Jul; Vol. 30 (4), pp. 685-9. - Publication Year :
- 1993
-
Abstract
- Lyophylized almond beta-glucosidase (EC 3.2.1.21) has been adsorbed onto Concanavalin A-Sepharose (CAS). The yield of the enzymatic units of the CAS-enzyme complex preparation was 131%. The values of the kinetic parameters of the free beta-glucosidase were: kM = 1.7 mM and Vmax = 330.1 U/mg protein. The immobilised form showed the following values: kM = 1.7 mM and Vmax = 402.6 U/mg protein. Both enzymatic forms showed essentially the same temperature- and pH-activity patterns (temperature optimum: 50 degrees C and pH optimum approx. 6.0), however, the pH stability of the CAS-enzyme complex at pH 6 was significantly higher than the beta-glucosidase in free solution.
Details
- Language :
- English
- ISSN :
- 1039-9712
- Volume :
- 30
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Biochemistry and molecular biology international
- Publication Type :
- Academic Journal
- Accession number :
- 8401325