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|Title:||Physicochemical properties of free and calcium alginate immobilized alkaline pectin lyase from Bacillus cereus|
|Keywords:||Pectin lyase;Immobilization;Bacillus cereus;Calcium alginate;Characterization|
|Abstract:||Purified pectin lyase from Bacillus cereus was successfully immobilized in alginate beads with a high binding efficiency of 84.55%. The optimal immobilization was achieved using 2.5% (w/v) alginate concentration. Both free and immobilized enzyme showed optimum pH of 10.0 and temperatures of 40 and 45°C respectively. Pectin lyase gave maximum activity at a substrate concentration of 0.5% w/v for free and 0.75% w/v for the immobilized enzyme and relatively similar Vmax values were obtained for both free (3.3 µmol/min) and immobilized pectin lyase (3.6 µmol/min). The Km for the immobilized pectin lyase (0.19 mg/ml) was slightly higher than that of the free (0.16 mg/ml) enzyme. The maximum inhibition of 50.2% was observed in the presence of Hg2+ ion for free pectin lyase and immobilized enzyme showed maximum inhibition of 67.32% in the presence of Na+ ion with statistically significant p-value (p < 0.05). Thermal stability was not significantly altered by immobilization. Thermal stability of free and immobilized pectin lyase was relatively similar at different temperatures. The immobilized pectin lyase retained almost 53% of its original activity up to 7th cycle. Furthermore, during storage at 4°C, immobilized pectin lyase retained relative activity of 79.77% and free enzyme retained 63.63% relative activity upto 35 days of storage, this indicated that the immobilization improved stability of the enzyme.|
|ISSN:||0975-0967 (Online); 0972-5849 (Print)|
|Appears in Collections:||IJBT Vol.18(4) [October 2019]|
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