[Immobilization of proteolytic complexes on pectin-containing carriers]

Area of Science:

• Biochemistry
• Materials Science
• Enzyme Technology

Background:

• Pectin is a natural polysaccharide with potential for developing novel biomaterials.
• Enzyme immobilization is crucial for enhancing enzyme stability and reusability.
• Proteolytic enzymes like pancreatin and protosubtilin are widely used in various industrial applications.

Purpose of the Study:

• To synthesize pectin-based sorbents for enzyme immobilization.
• To evaluate the efficiency of these sorbents for immobilizing pancreatin and protosubtilin.
• To characterize the properties of the immobilized enzyme preparations.

Main Methods:

• Synthesis of sorbents using pectin, formaldehyde, and melamine (PFM).
• Immobilization of pancreatin and protosubtilin onto PFM sorbents using Fe(III) ions.
• Enzyme activity assays using methyl ester of L-tryptophane as substrate.
• Determination of pH optimum and thermal stability of immobilized enzymes.

Main Results:

• PFM sorbents demonstrated excellent properties for enzyme immobilization.
• Immobilized pancreatin on PFM via Fe(III) exhibited high activity (79,000 mumole/g x h) with 91% activity yield.
• All immobilized preparations showed a shift in pH optimum towards the alkaline region.
• The thermostable fraction of immobilized enzymes maintained activity for extended periods at 60°C.

Conclusions:

• Pectin-based PFM sorbents are effective matrices for immobilizing proteolytic enzymes.
• Immobilization significantly enhances enzyme activity and stability, with potential for industrial applications.
• The developed immobilized enzyme preparations offer improved performance characteristics, including thermal stability.