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Title: Preparation and characterization of. beta. -D-glucosidase immobilized in calcium alginate

Conference ·
OSTI ID:6011936

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
Resource Relation:
Conference: 4. symposium on biotechnology in energy production and conservation, Gatlinburg, TN, USA, 11 May 1982
Country of Publication:
United States
Language:
English