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Title: Immobilized and stabilized cellulase and. beta. -D-glucosidase

Conference ·
OSTI ID:5407149

The major types of components of cellulase from Trichoderma reesei were adsorbed onto Concanavalin A immobilized on Sepharose 4B suggesting that they are glycoproteins. These components were covalently coupled to cyanogen bromide-activated Sepharose after aminoalkylation of their periodate-oxidized carbohydrate side chains to provide additional points of attachment of the enzyme to the support. Although there was only a 9% recovery of starting avicelase activity, the immobilzed enzyme catalyzed the hydrolysis of insoluble cellulose to glucose with greater efficiency than did free cellulase. The enzyme ..beta..-D-glucosidase from Aspergillus niger was also immobilized through its carbohydrate moiety by these methods. An increase in the thermal stability of the immobilized ..beta..-D-glucosidase preparations over the soluble enzyme was achieved if the enzyme was treated with glutaraldehyde prior to its adsorption on concanavalin A-Sepharose or if the enzyme immobilized on cyanogen bromide-activated Sepharose was subsequently treated with glutaraldehyde.

Research Organization:
Oak Ridge National Lab., TN (USA)
DOE Contract Number:
W-7405-ENG-26
OSTI ID:
5407149
Report Number(s):
CONF-820202-8; ON: DE82011440
Resource Relation:
Conference: AICHE 1982 national winter meeting, Orlando, FL, USA, 28 Feb 1982
Country of Publication:
United States
Language:
English