Immobilization of Lipase A from Candida antarctica onto Chitosan-Coated Magnetic Nanoparticles

Abstract

In this communication, lipase A from Candida antarctica (CALA) was immobilized by covalent bonding on magnetic nanoparticles coated with chitosan and activated with glutaraldehyde, labelled CALA-MNP, (immobilization parameters: 84.1% ± 1.0 for immobilization yield and 208.0 ± 3.0 U/g ± 1.1 for derivative activity). CALA-MNP biocatalyst was characterized by X-ray Powder Diffraction (XRPD), Fourier Transform Infrared (FTIR) spectroscopy, Thermogravimetry (TG) and Scanning Electron Microscope (SEM), proving the incorporation of magnetite and the immobilization of CALA in the chitosan matrix. Besides, the immobilized biocatalyst showed a half-life 8–11 times higher than that of the soluble enzyme at pH 5–9. CALA showed the highest activity at pH 7, while CALA-MNP presented the highest activity at pH 10. The immobilized enzyme was more active than the free enzyme at all studied pH values, except pH 7.

Hydrophilic Glyceryl Ferulates Preparation Catalyzed by Free Lipase B from <i>Candida antar</i><i>tica</i>

“…When Candida antarctica lipase-A CALA and Thermomyces lanuginosus Lipozyme TL 100L were used as biocatalysts, no FG was formed. Compared with CALA and Lipozyme TL100L, Candida antarctica lipase-B CALB showed the best activity for the reaction, which can be as-cribed to the higher enzyme activity of CALB 435 LU/mg than those of CALA 420 LU/mg and Lipozyme TL 100L 100 LU/mg 38,43,44 . Figure 1 shows that, when free CALB was used as catalyst and with time increasing from 2 h to 24 h, the FG yield and EF conversion gradually increased to 52.7…”

Advances in Recombinant Lipases: Production, Engineering, Immobilization and Application in the Pharmaceutical Industry

“…Dandavate et al [148] and Yilmaz et al [149] immobilized a Candida rugosa lipase onto the silica nanoparticles surface and glutaraldehyde-activated aminopropyl glass beads, resulting in easy recovery, and enzyme reuse for ester synthesis. In this context, when Candida antarctica lipase was immobilized on chitosan-coated magnetic nanoparticles of iron activated with glutaraldehyde for the production of the biolubricant ester, the biocatalyst gave half of the initial conversion after seven cycles of esterification [150].…”

Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method

“…The magnetic nanoparticles functionalized with APTES were produced following the methodology described by Monteiro et al (2019a). In 30 mL of deionized water, 2.5 g of FeSO 4…”

“…Adsorption Immobilization of RML on Fe 3 O 4 @APTES RML was immobilized on Fe 3 O 4 @APTES, called Fe 3 O 4 @APTES-RML (RML-MNPA), by adsorption. For this, 0.1 g of Fe 3 O 4 @APTES were suspended in 1 mL of sodium phosphate buffer solution (25 mM and pH 7) containing RML (enzymatic load: 10 mg/g support) (Monteiro et al, 2019a). The system was placed under constant agitation for 1 h at 25 • C. After that time, the biocatalyst was separated from the solution by magnetic decanting and washed with sodium phosphate buffer solution (25 mM and pH 7) until neutrality.…”

“…To analyze the effect of pH on the activity of the biocatalyst, free and immobilized lipase were resuspended in 1 mL of 25 mM buffer in the pH range ranging from 5 to 10 [sodium acetate (pH range 3.6-5.6), sodium phosphate (pH range 5.8-8.0), and sodium carbonate (pH range 8.9-10.8)] and using p-NPB as described earlier. The enzyme was incubated in each buffer for 15 min, and then the activity was measured (Monteiro et al, 2019a).…”