
Highly purified glutamine synthetase has been isolated from Chlorella and immobilized on BrCN-sepharose. Its residual activity was 25-35%. Immobilized glutamine synthetase showed far greater thermal stability than glutamine synthetase in solution. During immobilization pH optimum of the enzyme was shifted towards the alkaline area, maximum rate of the reaction was reduced and KM remained unaltered.
Enzyme Activation, Drug Stability, Glutamate-Ammonia Ligase, Temperature, Chlorella, Hydrogen-Ion Concentration, Enzymes, Immobilized
Enzyme Activation, Drug Stability, Glutamate-Ammonia Ligase, Temperature, Chlorella, Hydrogen-Ion Concentration, Enzymes, Immobilized
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