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.
Highlights
Chemical and enzymatic catalysts are both effective for industrial applications [1,2]; chemical catalysis possesses several drawbacks, such as high energy consumption, undesirable by-product formation and equipment corrosion [3,4]
The immobilization parameters were evaluated after 3 hours of immobilization, employing a protein load of 1 mg of protein per g of support for the hydrolysis of p-NPB (0.5 mM)
The enzyme immobilized on glutaraldehyde activated nanoparticles performed better than the non-activated nanoparticles, showing that glutaraldehyde plays a significant role on enzyme immobilization
Summary
Chemical and enzymatic catalysts are both effective for industrial applications [1,2]; chemical catalysis possesses several drawbacks, such as high energy consumption, undesirable by-product formation and equipment corrosion [3,4]. On the other hand, is not as energy-demanding due to the mild operating conditions. It is selective and specific, preventing undesired modifications of substrate and formation of toxic by-products, and it presents very low environmental impact [5,6,7,8,9]. CALB is the most extensively studied lipase in chemistry and fine chemistry [17], food technology [18] and bioenergy [19]; its crystalline structure was first reported in 1994 [20], whereas CALA had its crystalline structure more recently reported [21]. CALA has some useful properties to catalyze reactions, including high thermostability and the ability to tolerate a wide range of pHs [22,23]
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