Chemistry Reference
In-Depth Information
Chapter 5
On The Immobilization of
Candida antarctica
Lipase B onto Surface Modified Porous Silica
Gel Particles
Stephen J. Clarson, Richard A. Gross, Siddharth V. Patwardhan
and Yadagiri Poojari
5.1 Introduction
A variety of lipases have proven to be versatile and efficient biocatalysts and have
been utilized in transformations for esterification, transesterification, and ester hy-
drolysis reactions. Lipases have been widely employed in the food [
1
,
2
], perfume
[
3
], and detergent [
4
] industries. Lipases were also utilized as a catalyst in polymer
synthesis [
5
], for such systems as polyesters [
6
-
8
] and polycarbonates [
9
,
10
]. The
vast potential of these biocatalysts for use in industrial applications has been in-
creasingly recognized due to the high chemical selectivity, region selectivity, and
stereo selectivity of lipases under mild reaction conditions.
In recent years, the search for efficient methods and support materials for the im-
mobilization of lipases has emerged as an important field of interest. This is mainly
due to the need to recover and reuse the enzyme for commercial benefits. A variety
of techniques have been applied to immobilize lipases, including adsorption onto
solid supports [
11
], covalent attachment [
12
-
14
], and entrapment within polymers/
inorganic matrices [
15
,
16
]. In general, adsorption techniques are easy to perform,
but the binding of the enzyme is often weak and such biocatalysts lack the degree
of stabilization that it is possible to attain by entrapment or covalent attachment.
On the other hand, the enzyme entrapment leads to permanent loss of active sites
