Biologically active polymer supports based on cellulosic derivatives: synthesis and kinetic study

Area of Science:

• Biochemistry
• Polymer Chemistry
• Enzyme Technology

Background:

• Cellulose derivatives offer versatile platforms for biomolecule immobilization.
• Enzyme immobilization is crucial for enhancing enzyme stability and reusability.
• Carboxymethyl cellulose acid chloride and cellulose carbonate are key functionalized cellulose supports.

Purpose of the Study:

• To synthesize bioactive cellulose derivatives by coupling enzymes and antibiotics.
• To investigate the enzymatic activity and kinetics of amyloglucosidase immobilized on cellulose carbonate.
• To determine the effect of pH and temperature on immobilized enzyme performance.

Main Methods:

• Synthesis of carboxymethyl cellulose acid chloride and cellulose carbonate.
• Immobilization of amyloglucosidase onto cellulose carbonate.
• Enzymatic activity assays at varying pH and temperature.
• Kinetic analysis using Michaelis-Menten and Lineweaver-Burk plots.

Main Results:

• Bioactive cellulose derivatives were successfully synthesized.
• Immobilized amyloglucosidase on cellulose carbonate followed Michaelis-Menten kinetics.
• The Michaelis-Menten constant (Km) for immobilized amyloglucosidase at pH 8 was 9.1 mM.
• Activation energy for starch hydrolysis by immobilized enzyme was 21.8 kcals/mole.

Conclusions:

• Cellulose derivatives serve as effective supports for enzyme immobilization.
• Immobilized enzymes exhibit predictable kinetic behavior, even with restricted mobility.
• The characterized kinetic parameters provide insights for optimizing enzymatic processes using these novel materials.