skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Immobilization method for the recovery of cellulase used in cellulose conversion to ethanol

Technical Report ·
OSTI ID:5225230

Mixtures of cellulase and ..beta..-D-glucosidase when added to fermentation systems containing a yeast or bacterium enable the latter to utilize cellulose if they are inherently unable to do so. It is essential that the enzymes be recovered and recycled if such a system is to have commercial potential. The major components of Trichoderma reesei C30 cellulase have been adsorbed onto concanavalin A-Sepharose (CAS) to give maximum loadings of 2.7, 44.7, and 1.5 units g/sup -1/ dry CAS at 50/sup 0/C when measured with the substrates filter paper, carboxymethylcellulose and cellobiose, respectively. Cellulase immobilized by this method desorbs from the support in the presence of insoluble cellulose and interacts with the substrate. Cellulose is thus converted to ethanol by immobilized cellulase, ad ..beta..-D-glucosidase and Z, mobilis coentrapped within calcium alginate. It is proposed that reimmobilization of cellulase will take place if all the substrate is utilized and converted to ethanol by a co-immobilized yeast or bacterium. Immobilization of cellulase and ..beta..-D-glucosidase on CAS is unaffected by 10% (w/v) ethanol. There is also little effect of 10% ethanol on the activity of cellulase and ..beta..-D-glucosidase. The enzymes could be easily recovered from an ethanol containing medium by simple filtration, and reused. 15 references, 6 figures.

Research Organization:
Oak Ridge National Lab., TN (USA)
DOE Contract Number:
W-7405-ENG-26
OSTI ID:
5225230
Report Number(s):
CONF-840111-3; ON: DE84007515
Resource Relation:
Conference: 8. annual symposium on energy from biomass and wastes, Lake Buena Vista, FL, USA, 30 Jan 1984
Country of Publication:
United States
Language:
English