[A new method of immobilizing proteolytic enzymes in polymeric hydrogels]

Area of Science:

• Biochemistry
• Polymer Science
• Biotechnology

Context:

• Enzyme immobilization is crucial for biocatalysis and industrial applications.
• Developing efficient and stable enzyme immobilization techniques remains a challenge.
• Thermally responsive polymers offer unique properties for biomaterial development.

Purpose:

• To develop a novel one-step method for enzyme immobilization using a thermally reversible polymer.
• To optimize the entrapment of specific enzymes (trypsin and carboxypeptidase B) in composite gels.
• To evaluate the activity, stability, and application of the immobilized enzymes.

Summary:

• A one-step enzyme immobilization method was established using poly(N-vinyl-caprolactam) composite gels.
• High retention of original enzyme activities (80-90%) was achieved for carboxypeptidase B and trypsin.
• Immobilized enzymes exhibited enhanced activity across broader pH and temperature ranges.
• The immobilized enzyme granules were successfully applied in the production of human insulin from recombinant proinsulin.

Impact:

• This method provides a stable and efficient platform for enzyme immobilization.
• The enhanced stability and broader operational range of immobilized enzymes improve biocatalytic processes.
• Successful application in insulin production demonstrates the potential for pharmaceutical manufacturing.
• The use of thermally reversible polymers opens new avenues for enzyme engineering and biomaterial design.