In this paper, the A. fumigatus α-amylase had been immobilized onto zeolite/chitosan hybrid to improve its thermal-stabilization for industrial needs. The methods applied enzyme production, isolation, partial purification, immobilization, and characterization. The optimum temperatures of the native and immobilized enzymes were 50 and 55˚C, respectively. The native enzyme has KM of 3.478 ± 0.271 mg mL-1 substrate and Vmax of 2.211± 0.096 µmole mL-1 min-1, while the immobilized enzyme has KM value of 12.051 ± 4.949 mg mL-1 substrate and Vmax of 1.602 ± 0.576 µmole mL-1 min-1. The residual activity of the immobilized enzyme retained up 10.97% after fifth reuse cycles. The native enzyme has ΔGi of 104.35 ± 1.09 kJ mole-1 and t½ of 38.75 ± 1.53 min, while the immobilized enzyme has ΔGi of 108.03 ± 0.05 kJ mole-1 and t½ of 180.03 ± 3.31 min. According to the increase in half-life (t½), stability improvement of the A. fumigatusα-amylase was 4.65 times greater than the native enzyme. Thus, the zeolite/chitosan hybrid is used as a new supporting matrix for further enzyme immobilization to stabilize the enzymes. Doi: 10.28991/ESJ-2022-06-03-06 Full Text: PDF
The stability of enzymes which play an important role as biocatalysts in many industrial processes is a persistent challenge with significant impact on production costs. In this study, improvement of the stability of α-amylase obtained from Aspergillus fumigatus was attempted by immobilizing the enzyme onto zeolite using adsorption method. For purification, the isolated enzyme was subsequently subjected to centrifugation, fractionation, and dialysis. The native enzyme was found to have an optimum temperature of 50 °C, while the immobilized enzyme, the optimum temperature of 60 °C was found. The immobilized enzyme was found to have the K M value of 11.685 ± 0.183 mg mL−1 substrate and V max of 1.406 ± 0.049 μmol mL−1 min−1, while for the native enzyme, the K M value of 3.478 ± 0.271 mg mL−1 substrate and the V max of 2.211 ± 0.096 μmol mL−1 min−1 were obtained. Furthermore, the immobilized enzyme displays the ΔGi of 106.76 ± 0.00 kJ mol−1 and t ½ of 90.40 ± 0.00 min, while the native enzyme, the values obtained are ΔGi of 104.35 ± 1.09 kJ mol−1 and t½ of 38.75 ± 1.53 min. As can be seen, the t ½ of immobilized enzyme is 2.38 times longer than that of native enzyme, justifying a very significant stability enhancement of the enzyme as a result of. Another important finding is that the immobilized α-amylase enzyme was able to retain its activity as high as 13.80 ± 1.19% activity after five cycles, indicating its potential for industrial use.
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