[Modification and immobilization of beta-galactosidase]

Area of Science:

• Biochemistry
• Enzyme engineering
• Protein modification

Context:

• Enzyme immobilization is crucial for industrial applications.
• Dye modification can alter protein properties.
• Fungal enzymes offer unique characteristics.

Purpose:

• To modify beta-galactosidase from Curvularia inaequalis using a chlortriazin dye.
• To characterize the modified enzyme's properties, including activity and isoelectric point.
• To develop an immobilized enzyme preparation.

Summary:

• Beta-galactosidase from Curvularia inaequalis was covalently modified with active bright-orange KH chlortriazin dye.
• The modified enzyme incorporated two dye molecules per protein molecule, with six sulfuric groups affecting the isoelectric point but not catalytic activity.
• The resulting colored protein exhibited strong adsorption to anionites, enabling immobilization.

Impact:

• Provides a method for immobilizing beta-galactosidase with retained activity.
• Demonstrates the utility of dye modification for enzyme functionalization and immobilization.
• Potential for developing stable and reusable enzyme preparations for biotechnological processes.