Catalase immobilized in polypeptide/silica nanocomposites via emulsion and biomineralization with improved activities

Jhih Han Liou, Zih Hua Wang, I. Hsiu Chen, Steven S.S. Wang, Su Chun How, Jeng Shiung Jan

研究成果: Article同行評審

2 引文 斯高帕斯(Scopus)


Polypeptide-mediated silica mineralization is an attractive approach to prepare polypeptide/silica nanocomposites for enzyme immobilization. Herein, a facile approach for in situ immobilization of catalase (CAT) in polypeptide/silica nanocomposites is developed via the preparation of cross-linked polypeptide/enzyme microgels using an emulsion process followed by silica mineralization. The efficient protein immobilization under benign condition (25–28 °C, pH 7.0, 0.05 N) was evidenced by high immobilization yield (> 99%) and no protein leakage. Our data showed that the immobilized CAT exhibited prolonged reusability and storage stability compared to free one, suggesting that the composite networks not only provide suitable microenvironments to facilitate enzymatic reactions but also confine the enzyme macromolecules to prevent subunit dissociation. Star-shaped topology exhibited better coverage onto the enzyme than linear counterpart, leading to the superior reusability (relative activity >95% for 30 cycling number) and storage stability (relative activity >95% for 60 days) of the immobilized CAT (~ 14 mg/g of support). The substrate affinity and enzymatic reaction rate for the immobilized CAT were also influenced by silica content and polypeptide topology. This strategy may provide a feasible and inexpensive approach to fabricate polypeptide/silica nanocomposites, which would be promising materials in biotechnological fields such as enzyme immobilization.

頁(從 - 到)931-940
期刊International Journal of Biological Macromolecules
出版狀態Published - 2020 九月 15

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Economics and Econometrics
  • Energy(all)

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