Preparation and characterization of. beta. -D-glucosidase immobilized in calcium alginate
This study investigated the immobilization of ..beta..-D-glucosidase (E.C. 3.2.1.21) in calcium alginate gel spheres. The immobilized enzyme catalyzed the hydrolysis of cellobiose to glucose. During preparation of the enzyme-containing spheres, 49% of the initial activity was lost from the alginate slurry. There was a 37% retention of the enzyme activity that was actually immobilized within the spheres. This loss of activity upon immobilization may be caused by inhibition of the enzyme by calcium cations and alginate anions present in the gel. Mass transfer effects were apparently minimal in this system and were not responsible for the activity loss. Leakage of the enzyme from the spheres occurred during storage of the spheres occurred during storage of the spheres at 4/sup 0/C and during their incubation with stirring at 23/sup 0/C. Leakage was severe at pH 5.0 but could be prevented if the enzyme was treated with glutaraldehyde prior to immobilization.
- Research Organization:
- Oak Ridge National Lab., TN (USA)
- DOE Contract Number:
- W-7405-ENG-26
- OSTI ID:
- 6011936
- Report Number(s):
- CONF-820580-6; ON: DE83012587
- Country of Publication:
- United States
- Language:
- English
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59 BASIC BIOLOGICAL SCIENCES
ALDEHYDES
ALGINIC ACID
ALKALINE EARTH METAL COMPOUNDS
CALCIUM COMPOUNDS
CARBOHYDRATES
CATALYTIC EFFECTS
CELLULOSE
CHEMICAL PREPARATION
CHEMICAL REACTIONS
COLLOIDS
DECOMPOSITION
DISPERSIONS
ENZYMES
GELATION
GELS
GLUCOSE
GLUCOSIDASE
GLYCOSYL HYDROLASES
HEXOSES
HYDROLASES
HYDROLYSIS
IMMOBILIZED ENZYMES
LYSIS
MONOSACCHARIDES
O-GLYCOSYL HYDROLASES
ORGANIC COMPOUNDS
POLYSACCHARIDES
SACCHARIDES
SOLVOLYSIS
SPHERES
STORAGE
SYNTHESIS