Abstract
Immobilized enzymatic catalysts are widely used in the chemical and pharmaceutical industries. As Candida antarctica lipase B (CALB) is one of the more commonly used biocatalysts, we attempted to design an optimal lipase-catalytic system. In order to do that, we investigated the enantioselectivity and lipolytic activity of CALB immobilized on 12 different supports. Immobilization of lipase on IB-D152 allowed us to achieve hyperactivation (178%) in lipolytic activity tests. Moreover, the conversion in enantioselective esterification increased 43-fold, when proceeding with lipase-immobilized on IB-S861. The immobilized form exhibited a constant high catalytic activity in the temperature range of 25 to 55 °C. Additionally, the lipase immobilized on IB-D152 exhibited a higher lipolytic activity in the pH range of 6 to 9 compared with the native form. Interestingly, our investigations showed that IB-S500 and IB-S60S offered a possibility of application in catalysis in both organic and aqueous solvents. A significant link between the reaction media, the substrates, the supports and the lipase was confirmed. In our enzymatic investigations, high-performance liquid chromatography (HPLC) and the titrimetric method, as well as the Bradford method were employed.
Highlights
Over the past decade, there has been a rapid increase in the synthesis of chiral compounds and lipolysis reactions using enzymes immobilized on different supports
We present the results of comprehensive investigations of enantioselectivity and lipolytic activity of Candida antarctica lipase B (CALB) immobilized on 12 commercially available supports that differed in physical and chemical properties
Investigations of the enantioselectivity and lipolytic activity of CALB immobilized on polymeric carriers were described
Summary
There has been a rapid increase in the synthesis of chiral compounds and lipolysis reactions using enzymes immobilized on different supports. This enzyme technology is a promising solution that offers more environmentally-friendly and cost-effective methods to improve catalytic activity [1,2]. Lipases are among the most common biocatalysts used in the pharmaceutical and chemical industries. These proteins play an extremely important role in the chiral synthesis and enzymatic kinetic resolution of racemic compounds and in the hydrolysis and transesterification of oils.
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