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[Glucoamylase immobilized on AE-cellulose]
Prikladnaia Biokhimiia I Mikrobiologiia
|July 1, 1978
Summary
Immobilized glucoamylase enzyme shows enhanced activity when bound to AE-cellulose using glutaraldehyde. Optimal conditions for this enzyme immobilization include specific pH, temperature, and buffer concentrations for improved starch conversion.
Area of Science:
- Enzyme Technology
- Biochemistry
- Biomaterials
Background:
- Glucoamylase is a key enzyme for starch hydrolysis.
- Enzyme immobilization enhances stability and reusability.
- AE-cellulose offers a suitable matrix for covalent enzyme binding.
Purpose of the Study:
- To immobilize glucoamylase from Endomycopsis species 20-9 onto AE-cellulose.
- To optimize immobilization conditions for maximal enzyme activity.
- To investigate the effect of substrate and product on immobilized enzyme performance.
Main Methods:
- Covalent binding of glucoamylase to AE-cellulose using glutaraldehyde.
- Assaying enzyme activity under varying pH, buffer concentration, and temperature.
- Evaluating the impact of immobilization time on enzyme preparations.
- Assessing the influence of starch and glucose on immobilized enzyme activity.
Main Results:
- Optimal immobilization achieved in 0.2 M Na-phosphate buffer at pH 5.0-7.0.
- Ideal temperature range for immobilization was 4-20°C over 4-24 hours.
- Immobilized glucoamylase activity increased nearly twofold in the presence of starch.
- Glucose did not significantly affect the activity of the immobilized enzyme.
Conclusions:
- Successful immobilization of glucoamylase on AE-cellulose was achieved.
- Defined optimal conditions enhance the efficiency of immobilized glucoamylase.
- The presence of starch positively influences immobilized glucoamylase activity, suggesting potential for improved industrial applications.