Immobilization of a Thermostable á-amylase on Calcium Alginate Beads from Bacillus Subtilis KIBGE-HAR
Aliya Riaz, Shah Ali Ul Qader, Abida Anwar, Samina Iqbal
Abstract
Aliya Riaz, Shah Ali Ul Qader, Abida Anwar, Samina Iqbal
Abstract
2 Abstract: Alpha-amylase from B. Subtilis KIBGE-HAR was partially purified by 40 % ammonium sulfate upto 7 folds and then immobilized by entrapment in calcium-alginate beads. The catalytic properties of the immobilized a-amylase were compared with that of the free enzyme. The optimum pH of the free enzyme was 7.0 while that of immobilized enzyme was pH 7.5. The optimum temperature for free and immobilized enzyme was 60c and 70c respectively. The activity yield of the immobilized enzyme was 65 %. A substrate maximum for immobilized enzyme was changed from 2 % to 3%. Incubation time for enzyme-substrate reaction was remained same i.e. 5 minutes for the free and immobilized a-amylase.
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2 Abstract: Alpha-amylase from B. Subtilis KIBGE-HAR was partially purified by 40 % ammonium sulfate upto 7 folds and then immobilized by entrapment in calcium-alginate beads. The catalytic properties of the immobilized a-amylase were compared with that of the free enzyme. The optimum pH of the free enzyme was 7.0 while that of immobilized enzyme was pH 7.5. The optimum temperature for free and immobilized enzyme was 60c and 70c respectively. The activity yield of the immobilized enzyme was 65 %. A substrate maximum for immobilized enzyme was changed from 2 % to 3%. Incubation time for enzyme-substrate reaction was remained same i.e. 5 minutes for the free and immobilized a-amylase.
Key concepts: Calcium alginate, Bacillus subtilis, Amylase, Immobilized enzyme, Substrate (aquarium), Chemistry, Enzyme, Enzyme assay