Entrapment of concanavalin A-glycoenzyme complexes in calcium alginate gels.

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 Bioeng

authors

Husain Q,Iqbal J,Saleemuddin M

doi

10.1002/bit.260270803

subject

Has Abstract

pub_date

1985-08-01 00:00:00

pages

1102-7

issue

8

eissn

0006-3592

issn

1097-0290

journal_volume

27

pub_type

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