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?-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride.


ABSTRACT: Enzyme immobilization is one of the most important techniques for industrial applications. It makes the immobilized enzyme more stable and advantageous than the free form in different aspects. ?-Amylase was immobilized on 4% cyanuric chloride-activated amidoximated acrylic fabric at pH 7.0 with (79%) maximum efficiency. A field emission scanning electron microscope and Fourier transform infrared were used to confirm the immobilization process. Even after being recycled 10 times, the immobilized enzyme lost just 28% of its initial activity. Owing to immobilization, the pH of the soluble ?-amylase was shifted from 6.0 to 6.5. The immobilized ?-amylases showed thermal stability at 60°C, and became more resistant to heavy metal ions. The k m values of the immobilized and soluble ?-amylases were 9.6 and 3.8 mg starch ml-1, respectively. In conclusion, this method shows that the immobilized ?-amylase proved to be more efficient than its soluble form, and hence could be used during saccharification of starch.

SUBMITTER: Almulaiky YQ 

PROVIDER: S-EPMC6281920 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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Enzyme immobilization is one of the most important techniques for industrial applications. It makes the immobilized enzyme more stable and advantageous than the free form in different aspects. α-Amylase was immobilized on 4% cyanuric chloride-activated amidoximated acrylic fabric at pH 7.0 with (79%) maximum efficiency. A field emission scanning electron microscope and Fourier transform infrared were used to confirm the immobilization process. Even after being recycled 10 times, the immobilized  ...[more]

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