Premium
Properties of cellulase immobilized on agarose gel with spacer
Author(s) -
Chimanage Patoomporm,
Kashiwagi Yutaka,
Magae Yumi,
Ohta Teruo,
Sasaki Takashi
Publication year - 1986
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260281215
Subject(s) - cellulase , agarose , sepharose , chemistry , cyanogen bromide , hydrolysis , trichoderma viride , chromatography , cellobiose , cellulose , immobilized enzyme , cyanogen , substrate (aquarium) , biochemistry , enzyme , organic chemistry , biology , food science , ecology , peptide sequence , gene
Cellulase produced by fungus Trichoderma viride was immobilized on agarose beads (Sepharose 4B) activated by cyanogen bromide and also on activated agarose beads that contained spacer arm (activated CH‐Sepharose 4B and Affi‐Gel 15). The CMCase activity retained by immobilized cellulase on activated Sepharose containing the spacer tended to be higher than that immobilized without spacer, although the extent of protein immobilization was lower. Also, the higher substrate specificity for cellulase immobilized on beads with spacer was obtained for cellobiose, acid‐swollen cellulose, or cellulose powder. The hydrolysis product from their substrates was mainly glucose.