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Entrapment of concanavalin A‐glycoenzyme complexes in calcium alginate gels
Author(s) -
Husain Qayyum,
Iqbal Jawaid,
Saleemuddin M.
Publication year - 1985
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.260270803
Subject(s) - concanavalin a , invertase , chemistry , entrapment , calcium alginate , immobilized enzyme , sucrose , chromatography , glucose oxidase , hydrolysis , calcium , enzyme , biochemistry , organic chemistry , in vitro , medicine , surgery
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, η, 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 η. A column containing crosslinked concanavalin A‐invertase complex entrapped in alginate beads retained the ability to completely hydrolyze 1 M sucrose even after continuous operation for over four months.