Improved performance of lipases immobilized on heterofunctional octyl-glyoxyl agarose beads

Abstract

A new heterofunctional support, octyl-glyoxyl agarose, is proposed in this study.

Chemical amination of lipases improves their immobilization on octyl-glyoxyl agarose beads

“…However, in the previous report, a percentage of the immobilized enzyme molecules were not able to establish a covalent linkage with the support [39]. In other cases, the enzyme activity decreased significantly upon incubation at pH 10 necessary to get the enzyme-support covalent attachment [39].…”

“…As glyoxyl groups cannot directly immobilize proteins at neutral pH values [42], the use of this support at low ionic strength and neutral pH values has permitted the first immobilization of the lipases via interfacial activation [39]. Later, by incubation at pH 10, covalent attachments between immobilized enzyme molecules and the very close glyoxyl groups permitted the establishment of covalent linkages, and that way the enzyme cannot be desorbed under any experimental condition [39].…”

“…The new heterofunctional supports are easily prepared by the conversion of octyl-agarose in a heterofunctional octylglyoxyl support, by oxidation with sodium periodate of the diols of the support produced during industrial preparation of the crosslinked agarose [39]. As glyoxyl groups cannot directly immobilize proteins at neutral pH values [42], the use of this support at low ionic strength and neutral pH values has permitted the first immobilization of the lipases via interfacial activation [39].…”

“…In other cases, the enzyme activity decreased significantly upon incubation at pH 10 necessary to get the enzyme-support covalent attachment [39].…”

“…However, the enzymes adsorbed in this way may be released to the medium if exposed to organic solvents or detergents [38]. In this context, it has been recently shown that the lipase immobilization on heterofunctional octyl-glyoxyl supports is a simple way of preparing lipase biocatalysts useful in any reaction medium [39]. Acyl-glyoxyl supports have been used in diverse applications [40,41].…”