Invertase immobilization via its carbohydrate moiety.

Abstract:

:After periodate oxidation of its glycosidic component, invertase was covalently bound onto three types of modified solid supports: glycidyl methacrylate, styrene-divinylbenzene copolymers, and bead cellulose. Direct reaction of the invertase aldehyde groups that were formed with amino groups of the support and use of the modified Ugi reaction have been employed as immobilization procedures. Apart from binding methods, the important effects of the buffer, support, conditions of periodate oxidation, and the length of the spacer on the activity of the enzyme conjugate have been investigated. Superior conjugate activity was obtained, via modified Ugi reaction, by the immobilization of a suitably oxidized invertase to a styrene-divinylbenzene copolymer having free amino groups.

journal_name

Biotechnol Bioeng

authors

Marek M,Valentová O,Kás J

doi

10.1002/bit.260261011

subject

Has Abstract

pub_date

1984-10-01 00:00:00

pages

1223-6

issue

10

eissn

0006-3592

issn

1097-0290

journal_volume

26

pub_type

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