Immobilization of Proteins on Highly Activated Glyoxyl Supports: Dramatic Increase of the Enzyme Stability via Multipoint Immobilization on Pre-existing Carriers

Author(s): Gloria Fernández-Lorente, Fernando Lopez-Gallego, Juan M Bolivar, Javier Rocha-Martin, Sonia Moreno-Perez, Jose M. Guisan.

Journal Name: Current Organic Chemistry

Volume 19 , Issue 17 , 2015

Become EABM
Become Reviewer

Abstract:

The binding of enzymes on carriers with a high degree of activation with glyoxyl groups is an excellent method for improving enzyme stability by multipoint covalent attachment on a pre-existing carrier. Glyoxyl groups are short aliphatic aldehyde groups (Support – O-CH2 – CHO) that can be obtained by periodate oxidation of glyceryl groups (Support –O-CH2-CHOH-CH2OH). The unique features of glyoxyl groups are as follows:

a.- The immobilization of enzymes through their amino groups has to occur via multipoint attachment.

b.- The glyoxyl groups are stable at pH 10, which allows for the participation of Lys in the immobilization process.

c.- The glyoxyl groups are very stable at pH 10, which allows for a long-term incubation between the immobilized enzyme and the activated support to promote a very intense enzyme-support multipoint covalent attachment.

Using this protocol, more than 100 industrial enzymes were highly stabilized. In many cases, stabilizations of greater than 1000-fold compared with immobilized derivatives generated by conventional methods were obtained. Although dramatic stabilization was achieved, the immobilized enzymes maintained only 50 to 90 % of the catalytic activity of the corresponding soluble enzyme. Stabilization of industrial enzymes is a key step in immobilization protocols. Enzymes are immobilized for use at industrial scales for a number of reaction cycles.

Keywords: Immobilization-stabilization of enzymes, enzyme-support multipoint covalent attachment, glyoxyl-agarose supports.

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 19
ISSUE: 17
Year: 2015
Page: [1719 - 1731]
Pages: 13
DOI: 10.2174/138527281917150806125708
Price: $58

Article Metrics

PDF: 21
HTML: 2
EPUB: 1
PRC: 1