Abstract:
:Glucose oxidase, invertase, and amyloglucosidase were entrapped in calcium alginate gels as concanavalin A complexes in order to prevent the leaching out of the enzymes from the porous matrix. The free as well as the gel-entrapped concanavalin A-glycoenzyme complexes exhibited a relatively high effectiveness factor, eta, indicating good accessibility to the substrates. Concanavalin A-invertase complex exhibited marked broadening of pH-activity and temperature-activity profiles and was highly resistant to temperature inactivation even after entrapment in the alginate beads. It was possible to entrap considerable quantities of invertase as concanavalin A complex in the beads without a marked decrease in eta. A column containing crosslinked concanavalin A-invertase complex entrapped in alginate beads retained the ability to completely hydrolyze 1M sucrose even after continuous operation for over four months.
journal_name
Biotechnol Bioengjournal_title
Biotechnology and bioengineeringauthors
Husain Q,Iqbal J,Saleemuddin Mdoi
10.1002/bit.260270803subject
Has Abstractpub_date
1985-08-01 00:00:00pages
1102-7issue
8eissn
0006-3592issn
1097-0290journal_volume
27pub_type
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