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Optimization of protease immobilization by covalent binding using glutaraldehyde

H J Chae1, M J In, E Y Kim

  • 1R&D Center, Daesang Corp., Kyoungki, Korea.

Applied Biochemistry and Biotechnology
|October 21, 1998
PubMed
Summary

Researchers optimized covalent immobilization of the protease Flavourzyme using Lewatit R258-K and glutaraldehyde. Optimal conditions yielded high enzyme activity and recovery, crucial for industrial applications.

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Area of Science:

  • Biocatalysis and Enzyme Technology
  • Protein Immobilization Techniques
  • Chemical Engineering

Background:

  • Enzyme immobilization is vital for enzyme reusability and stability in industrial processes.
  • Proteases, like Flavourzyme, are widely used in food and detergent industries.
  • Covalent binding offers robust enzyme-carrier attachment.

Purpose of the Study:

  • To investigate the covalent immobilization of the protease Flavourzyme onto various carriers.
  • To optimize immobilization conditions for enhanced enzyme activity and recovery yield.
  • To identify the most effective carrier and immobilization parameters.

Main Methods:

  • Screening of carriers for Flavourzyme immobilization, with Lewatit R258-K selected.
  • Activation of Lewatit R258-K using glutaraldehyde.

Related Experiment Videos

  • Optimization of buffer concentrations, carrier loading, and enzyme loading.
  • Activity assays to determine immobilized enzyme performance.

    • Main Results:

    • Lewatit R258-K activated with glutaraldehyde showed the highest immobilized enzyme activity.
    • Optimal buffer concentrations for activation and immobilization were 500 mM and 50 mM, respectively.
    • Optimal enzyme and carrier loadings were determined as 1.8 mg enzyme/mL and 0.6 g resin/mL, respectively, balancing activity and recovery.

    Conclusions:

    • Successful covalent immobilization of Flavourzyme was achieved using optimized conditions.
    • The study provides optimal parameters for maximizing immobilized Flavourzyme activity and recovery yield.
    • This research contributes to efficient enzyme utilization in industrial biocatalysis.