Abstract
In this work, poly(n-butylamino)(allylamino)phosphazene (PBAP) was synthesized and tethered on polypropylene microporous membrane (PPMM) with the aim of offering a biocompatible and, at the same time, moderately hydrophobic microenvironment to lipase for the first time. Lipase from Candida rugosa was used and the influence of membrane surface conditions on the activities of immobilized lipases was evaluated. Water contact angle measurement as well as field emission scanning electron microscopy were used to characterize the morphology of the modified membranes. The results showed an improvement in the adsorption capacity (26.0 mg/m2) and activity retention (68.2%) of the immobilized lipases on the PBAP-modified PPMM. Moreover, the lipases immobilized on the modified PPMM showed better thermal and pH stability.
Highlights
Lipases are enzymes with the capability to catalyze a wide range of reactions such as hydrolysis, trans-esterification, aminolysis and enantiomer resolution, and they are very promising in the food, pharmaceutical, and detergent industries [1,2,3]
Special emphasis has been put on immobilizing lipases onto hydrophobic support surfaces in recent years, which is based on the assumption that the active state of lipases can be stabilized by the hydrophobic interaction between the hydrophobic active center of lipases and the hydrophobic support [12,13,14,15]
We systematically studied the structural rearrangements, immobilization kinetics and protein aggregation of lipase from Candida rugosa absorbed on a wettability-tailored surface, and concluded that a support with proper hydrophobicity is of vital importance for obtaining a highly efficient immobilized lipase [16]
Summary
Lipases are enzymes with the capability to catalyze a wide range of reactions such as hydrolysis, trans-esterification, aminolysis and enantiomer resolution, and they are very promising in the food, pharmaceutical, and detergent industries [1,2,3]. One remarkable characteristic of lipases is their activation facing a hydrophobic interface, which can induce conformational rearrangements and generate the “open state” of lipases and improve lipases’. Special emphasis has been put on immobilizing lipases onto hydrophobic support surfaces in recent years, which is based on the assumption that the active state of lipases can be stabilized by the hydrophobic interaction between the hydrophobic active center of lipases and the hydrophobic support [12,13,14,15]. We systematically studied the structural rearrangements, immobilization kinetics and protein aggregation of lipase from Candida rugosa absorbed on a wettability-tailored surface, and concluded that a support with proper hydrophobicity is of vital importance for obtaining a highly efficient immobilized lipase [16]
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