Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions

Immobilization of the Peroxygenase from Agrocybe aegerita. The Effect of the Immobilization pH on the Features of an Ionically Exchanged Dimeric Peroxygenase

“…This drastic difference of enzyme stability of enzymes immobilized in the same ion exchanger, but at different pH values, could be related to two factors: a different orientation of the enzyme in the support (involving different areas of the protein in the absorption when the immobilization pH changes and the ionization of the enzyme groups is altered) or the immobilization of different enzyme forms induced by the pH value [48,61,102]. The immobilization of lipases via interfacial activation on the same support (also a reversible immobilization protocol), but under different conditions, has proved to give different enzyme conformations, which are maintained after the immobilization [104][105][106]. The thermal inactivation courses of the 3 biocatalysts of the enzyme immobilized in MANAE agarose beads are shown in Figure 11.…”

“…ferent areas of the protein in the absorption when the immobilization pH changes and the ionization of the enzyme groups is altered) or the immobilization of different enzyme forms induced by the pH value [48,61,102]. The immobilization of lipases via interfacial activation on the same support (also a reversible immobilization protocol), but under different conditions, has proved to give different enzyme conformations, which are maintained after the immobilization [104][105][106]. In any case, this effect of the immobilization pH, even when the enzyme is reversibly immobilized, shows the significance of this parameter when preparing immobilized biocatalysts with this immobilization strategy.…”

Pristine and Poly(Dimethylsiloxane) Modified Multi-Walled Carbon Nanotubes as Supports for Lipase Immobilization

“…This is directly related to the fact that PDMS provides the hydrophobic nature of the surface and consequently the hydrophobic microenvironment for the immobilized lipase. In these conditions, lipase might undergo a phenomenon called interfacial activation, whichis based on opening of the polypeptide lid of the enzyme active site, leading to improvement of the activity of the immobilized enzyme [56,57]. Finally, significant enhancement of enzyme thermal stability (up to 50% higher relative activity, as compared to free enzyme) and reduction ofinactivation constant of immobilized enzymes are related to the fact that immobilization providesa protective environment for the enzyme molecules, whichreduces conformational changes of the enzyme structure in the presence of long-heat exposure.…”

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

“…In the case of lipases, all these advantages may be obtained by a very simple immobilization strategy. Using lipases, the best protocol to have an improved biocatalyst is just a simple physical adsorption of the enzyme on the support: the interfacial activation of the lipases versus support Although lipase immobilization on hydrophobic supports may be achieved under a wide range of conditions, it has been recently shown that the immobilization medium conditions may greatly alter the properties of the immobilized lipases, at least when using some lipases [366][367][368]. This may be considered as an advantage, as it permits the modulation of the enzyme properties using a single immobilization support [61], or as a problem, as this means that changes in the immobilization medium composition may produce biocatalysts with different catalytic properties (activity, specificity, stability), and this may be in some instances hard to control (Figure 19).…”

“…It has been widely showed that changes in the immobilization protocol or the physical or chemical modification of the immobilized lipases may greatly alter the enzyme features [61]. Using the same immobilization mechanism, e.g., the interfacial activation of the lipase versus hydrophobic support surfaces [81,360], it has been shown that the change of the support features greatly affects the final enzyme specificity, activity and stability [425][426][427]-even immobilization of the same enzyme using the same hydrophobic support, but just changing the immobilization conditions gives very different enzyme properties [366][367][368] (Figure 19). In fact, it has been recently shown that the lipase from T. lanuginosus immobilized on a hydrophobic support under certain conditions was a strict 1,3 selective enzyme, being unable to hydrolyze 2-monoglycerides, while the enzyme immobilized under other conditions can hydrolyze 2-monoglycerides, and that also depended on the immobilization support [428,429].…”