Development of immobilized cellulase

Technical Report · Sun Aug 01 00:00:00 EDT 1982

OSTI ID:5246541

Luther, M A; Halbert, D J

The immobilization of cellulase from the fungus Trichoderma reesei on the surface of calcium alginate gel spheres was investigated. The immobilized cellulase catalyzed the hydrolysis of cellulose to glucose. The linking agents, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) and glutaraldehyde, decreased free-enzyme activity by 95%, and the maximum observed retention of cellulase activity after immobilization was 2%. Leakage of enzyme from the support was observed. A fivefold increase in glucose production was seen after the addition of ..beta..-glucosidase-impregnated spheres to the cellulase spheres, suggesting that cellobiose may be accumulating during the reaction. A simple economic analysis suggested that the immobilized-enzyme activity per unit volume might have to be increased by a factor of fifty to become competitive with the free-enzyme process.

• Research Organization: Oak Ridge National Lab., TN (USA); Massachusetts Inst. of Tech., Oak Ridge, TN (USA). School of Chemical Engineering Practice
• DOE Contract Number: W-7405-ENG-26
• OSTI ID: 5246541
• Report Number(s): ORNL/MIT-346; ON: DE82019896
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ALGINATES
CARBOHYDRATES
CELLULASE
CELLULOSE
CHEMICAL REACTIONS
COLLOIDS
DECOMPOSITION
DISPERSIONS
ECONOMICS
ENZYME ACTIVITY
ENZYMES
FUNGI
GELS
GLYCOSYL HYDROLASES
HYDROLASES
HYDROLYSIS
IMMOBILIZED ENZYMES
LYSIS
O-GLYCOSYL HYDROLASES
ORGANIC COMPOUNDS
PLANTS
POLYSACCHARIDES
SACCHARIDES
SOLVOLYSIS
SPHERES
TRICHODERMA