Invertase immobilization via its carbohydrate moiety

✍ Scribed by M. Marek; O. Valentová; J. Káš

• Publisher: John Wiley and Sons
• Year: 1984
• Tongue: English
• Weight: 371 KB
• Volume: 26
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260261011

✦ Synopsis

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 suitablyoxidized invertase to a styrene-divinylbenzene copolymer having free amino groups.