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Related Experiment Video

Updated: May 8, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
11:16

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization

Published on: July 11, 2012

Fouling-induced enzyme immobilization for membrane reactors.

Jianquan Luo1, Anne S Meyer1, Gunnar Jonsson1

  • 1Department of Chemical and Biochemical Engineering, Center for BioProcess Engineering, Technical University of Denmark, Building 229, DK-2800 Kgs. Lyngby, Denmark.

Bioresource Technology
|September 3, 2013
PubMed
Summary

A new enzyme immobilization technique uses membrane fouling to enhance enzyme reusability and reduce product inhibition in enzymatic membrane reactors. This method offers improved stability and loading, particularly in reverse mode.

Keywords:
BiocatalysisEMREnzyme immobilizationProteinUltrafiltration

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Published on: September 23, 2013

Area of Science:

  • Biotechnology
  • Chemical Engineering
  • Materials Science

Background:

  • Enzyme immobilization is crucial for developing efficient enzymatic membrane reactors (EMRs).
  • Traditional methods face challenges in enzyme loading, stability, and reusability.
  • Membrane fouling, often considered detrimental, can be leveraged for enzyme immobilization.

Purpose of the Study:

  • To propose and evaluate a novel enzyme immobilization method using controlled membrane fouling.
  • To compare enzyme immobilization efficiency and performance in two membrane orientations (normal and reverse mode).
  • To assess the impact of this immobilization strategy on enzyme reusability and product inhibition.

Main Methods:

  • Enzyme immobilization via adsorption and entrapment during membrane fouling.
  • Utilizing two membrane orientations: skin layer facing feed (normal mode) and support layer facing feed (reverse mode).
  • Immobilizing alcohol dehydrogenase (ADH) and glutamate dehydrogenase (GDH) to test the method.
  • Analyzing fouling characteristics using filtration models and comparing EMR performance.

Main Results:

  • Reverse mode allowed higher enzyme loading and enhanced enzyme stability compared to normal mode.
  • Irreversible fouling (pore blocking) was more pronounced in the support layer than the skin layer.
  • Enzymes immobilized in the membrane support (reverse mode) showed improved reusability (ADH) and reduced product inhibition (GDH) versus free enzymes.
  • Permeate flux was higher in the normal mode.

Conclusions:

  • Enzyme immobilization by promoting membrane fouling is a viable and simple strategy.
  • The reverse mode offers significant advantages for enzyme loading, stability, and reactor performance.
  • This novel EMR design enhances enzyme reusability and mitigates product inhibition, paving the way for more robust biocatalytic processes.