Entrapment of enzymes using organo-functionalized polysiloxane copolymers

Area of Science:

• Biochemistry
• Polymer Science
• Biotechnology

Background:

• Enzyme immobilization is crucial for biocatalysis and biosensor development.
• Previous methods for enzyme entrapment have limitations in yield and enzyme activity retention.

Purpose of the Study:

• To investigate the entrapment of urease and invertase enzymes in organo-functionalized polysiloxane copolymers.
• To evaluate the biological activity, stability, and yield of entrapped enzymes compared to solution-based counterparts and other techniques.

Main Methods:

• Enzyme entrapment using polysiloxane copolymers synthesized from 3-aminopropyltriethoxysilane and tetraethylorthosilicate.
• Assessment of enzyme activity, yield, and stability (pH, temperature, substrate inhibition, operational, and storage) for both urease and invertase.

Main Results:

• Urease entrapment in the polysiloxane copolymer resulted in significantly higher yield and activity retention compared to other methods, with entrapped urease showing 36% greater activity than its solution form.
• The entrapment process enhanced urease stability against pH, temperature, and high urea concentrations, also improving operational and storage stability.
• Invertase retained two-thirds of its solution activity upon entrapment, though with a lower yield than urease.

Conclusions:

• Organo-functionalized polysiloxane copolymers provide an effective matrix for enzyme immobilization, enhancing enzyme stability and activity.
• The study highlights the potential of this copolymer system for improved enzyme applications.
• Further research is suggested to explore the interplay between protein and polymer during the entrapment process.