Immobilization and stabilization of invertase using specific polyclonal antibodies

Area of Science:

• Biochemistry
• Enzymology
• Protein Chemistry

Background:

• Baker's yeast invertase is a crucial enzyme in biotechnological processes.
• Enzyme immobilization is key to enhancing stability and reusability.
• Antibody-enzyme interactions can modulate enzyme activity and properties.

Purpose of the Study:

• To investigate the effect of antisera on baker's yeast invertase activity.
• To develop methods for immobilizing invertase using antibody-enzyme adducts.
• To evaluate the activity and thermal stability of immobilized invertase.

Main Methods:

• Raising antisera in rabbits against baker's yeast invertase.
• In vitro enzyme activity assays.
• Immobilization of invertase via antibody-antigen complex formation and Sepharose binding.
• Cross-linking of immobilized enzyme with glutaraldehyde.

Main Results:

• Antisera significantly activated invertase in vitro.
• Antibodies were directed against glycosyl residues of the enzyme.
• Immobilized invertase preparations retained high activity.
• Immobilized invertase exhibited enhanced thermal stability, further improved by glutaraldehyde cross-linking.

Conclusions:

• Antibody-enzyme interactions can be harnessed to activate and stabilize invertase.
• Immobilization strategies using antibody-antigen complexes offer a viable method for enzyme preparation.
• The enhanced thermal stability of immobilized invertase broadens its potential industrial applications.