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Nanoporous Phyllosilicate Assemblies for Enzyme Immobilization.

Shuang Mei1,2, Jiafu Shi3,2,4, Shaohua Zhang1,2

  • 1Key Laboratory for Green Chemical Technology of Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China.

ACS Applied Bio Materials
|January 12, 2022
PubMed
Summary
This summary is machine-generated.

New nanoporous copper phyllosilicate (L-CuSiO3) assemblies effectively immobilize horseradish peroxidase (HRP) for wastewater treatment. This adsorbent offers high stability, enzyme loading, and recyclability, enhancing phenol removal efficiency.

Keywords:
Copper phyllosilicate (L-CuSiO3)enzyme immobilizationhorseradish peroxidasenanoporous assemblyphenol removal

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Area of Science:

  • Materials Science
  • Environmental Science
  • Biotechnology

Background:

  • Enzyme immobilization via physical/chemical adsorption is effective but requires adsorbents with enhanced stability, capacity, and low leaching.
  • Developing novel adsorbents is crucial for efficient enzyme immobilization in industrial applications like wastewater treatment.

Purpose of the Study:

  • To prepare and characterize nanoporous two-dimensional (2D) copper phyllosilicate (L-CuSiO3) assemblies as adsorbents for enzyme immobilization.
  • To evaluate the performance of immobilized horseradish peroxidase (HRP) on L-CuSiO3 for phenol removal from wastewater.

Main Methods:

  • Synthesis of nanoporous 2D L-CuSiO3 assemblies.
  • Immobilization of HRP onto L-CuSiO3 using Cu(II)-arginine coordination.
  • Characterization of adsorbent properties (structural stability, surface area, enzyme loading capacity, leaching ratio).
  • Assessment of the immobilized enzyme's activity and stability in phenol degradation.

Main Results:

  • L-CuSiO3 assemblies exhibit robust structural stability due to Si-O-Si and Si-O-Cu bonds.
  • High specific surface area (611.7 cm3 g-1) enabled fast and high HRP loading (140 mg g-1 in 4 h).
  • Stable enzyme attachment via Cu(II)-arginine coordination resulted in <10% leaching.
  • HRP-loaded L-CuSiO3 showed 2-fold higher activity and improved stability compared to conventional supports, efficiently removing phenol.

Conclusions:

  • Nanoporous L-CuSiO3 assemblies are promising adsorbents for enzyme immobilization, offering superior structural stability, high enzyme loading, and low leaching.
  • The developed biocatalyst demonstrates enhanced performance for phenol removal in wastewater treatment, highlighting potential for industrial biocatalysis.
  • The ease-of-recycling feature of L-CuSiO3 assemblies further enhances their applicability in sustainable industrial processes.