Abstract

Silica xerogels have been proposed as a potential support to immobilize enzymes. Improving xerogels’ interactions with such enzymes and their mechanical strengths is critical to their practical applications. Herein, based on the mussel-inspired chemistry, we demonstrated a simple and highly effective strategy for stabilizing enzymes embedded inside silica xerogels by a polydopamine (PDA) coating through in-situ polymerization. The modified silica xerogels were characterized by scanning and transmission electron microscopy, Fourier tranform infrared spectroscopy, X-ray diffraction, X-ray photoelectron spectroscopy and pore structure analyses. When the PDA-modified silica xerogels were used to immobilize enzymes of Candida antarctica lipase B (CALB), they exhibited a high loading ability of 45.6 mg/gsupport, which was higher than that of immobilized CALB in silica xerogels (28.5 mg/gsupport). The immobilized CALB of the PDA-modified silica xerogels retained 71.4% of their initial activities after 90 days of storage, whereas the free CALB retained only 30.2%. Moreover, compared with the immobilization of enzymes in silica xerogels, the mechanical properties, thermal stability and reusability of enzymes immobilized in PDA-modified silica xerogels were also improved significantly. These advantages indicate that the new hybrid material can be used as a low-cost and effective immobilized-enzyme support.

Highlights

  • Compared with the SiO2 –CH3 –Candida antarctica lipase B (CALB), the results showed that PDA-modified SiO2 –CH3 –CALB had better mechanical properties, thermal stability, storage stability and reusability

  • SiO2–CH3–CALB had changed due to the uniformly distributed deposition of polydopathe microstructure of SiO2 –CH3 –CALB had changed due to the uniformly distributed mine within the structure of the xerogel [35]. These results indicate that a polydopamine deposition of polydopamine within the structure of the xerogel [35]

  • The immobilization of CALB in PDA-modified silica xerogels was successfully prepared by the self-polymerization of dopamine on the Si−O−Si network surfaces of silica xerogels

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Summary

Introduction

Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. The residual quinone on the surface of polydopamine or an intermediate displays a nucleophilic amino reaction that can be covalently connected with nucleophilic biological molecules, producing a polydopamine coating that is robust and durable [26] This provides a new way of improving the interactions between enzymes and supports, and of enhancing the mechanical properties of xerogels. Compared with the SiO2 –CH3 –CALB, the results showed that PDA-modified SiO2 –CH3 –CALB had better mechanical properties, thermal stability, storage stability and reusability This indicated that the new hybrid silica xerogel could be used as a low-cost and relatively effective immobilized-enzyme support. Catalysts 2021, 11, 1463 had better mechanical properties, thermal stability, storage stability and reusability

Characterization
XPS analyses of of
Strategy for Immobilizing CALB and Possible Mechanism
A macroscopic compression ex2 –CH
Transesterification and Reusability
The reaction diagram of of butyl butyl synthesis catalyzed by by
Comparison of Butyl Acetate Production Using Previous Lipase Biocatalysts
Experimental
Determination of Enzyme Loading
Assay of the CALB Activity
Thermal and Storage Stability of the Free CALB and Immobilized CALB
Mechanical Performance Tests
Conclusions
Full Text
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