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A Novel Bacterial Cellulose Aerogel Modified with PGMA via ARGET ATRP Method for Catalase Immobilization

A Novel Bacterial Cellulose Aerogel Modified with PGMA via ARGET ATRP Method for Catalase... Abstract Formation of Poly(Glycidyl Methacrylate) (PGMA) films on bacterial cellulose (BC) supports (aerogels) was achieved via activators regenerated by electron transfer for atom transfer radical polymerization (ARGET ATRP). Epoxy groups on PGMA were used for covalent coupling with catalase. Immobilized catalases on BC@PGMA were characterized by Fourier transform infrared spectroscopy (FTIR) and Typical scanning electron microscopy (SEM). The immobilized catalase amount reached a high value of 116 mg/g. Furthermore, the thermal, pH and storage stabilities of the immobilized catalase were improved significantly. After 10 use cycles, the BC@PGMA-catalase still retained approximately 63.5 % of the initial activity. This work demonstrates the potential of hierarchical nanomaterials for improving enzyme performance, leveraging the benefits of both nano- and macroscale supports. These results demonstrate that the BC@PGMA-catalase has high stability and good reusability, suggesting that the BC aerogel modified with PGMA may find applications in biotechnology and as biocatalyst. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Fibers and Polymers Springer Journals

A Novel Bacterial Cellulose Aerogel Modified with PGMA via ARGET ATRP Method for Catalase Immobilization

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References (20)

Publisher
Springer Journals
Copyright
2019 The Korean Fiber Society
ISSN
1229-9197
eISSN
1875-0052
DOI
10.1007/s12221-019-8650-4
Publisher site
See Article on Publisher Site

Abstract

Abstract Formation of Poly(Glycidyl Methacrylate) (PGMA) films on bacterial cellulose (BC) supports (aerogels) was achieved via activators regenerated by electron transfer for atom transfer radical polymerization (ARGET ATRP). Epoxy groups on PGMA were used for covalent coupling with catalase. Immobilized catalases on BC@PGMA were characterized by Fourier transform infrared spectroscopy (FTIR) and Typical scanning electron microscopy (SEM). The immobilized catalase amount reached a high value of 116 mg/g. Furthermore, the thermal, pH and storage stabilities of the immobilized catalase were improved significantly. After 10 use cycles, the BC@PGMA-catalase still retained approximately 63.5 % of the initial activity. This work demonstrates the potential of hierarchical nanomaterials for improving enzyme performance, leveraging the benefits of both nano- and macroscale supports. These results demonstrate that the BC@PGMA-catalase has high stability and good reusability, suggesting that the BC aerogel modified with PGMA may find applications in biotechnology and as biocatalyst.

Journal

Fibers and PolymersSpringer Journals

Published: Mar 1, 2019

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