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

Autor: Almulaiky YQ; Department of Biochemistry, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia.; Chemistry Department, Faculty of Applied Science, Taiz University, Taiz, Yemen., Aqlan FM; Chemistry Department, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia., Aldhahri M; Department of Biochemistry, Faculty of Science, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia.; Center of Nanotechnology, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia., Baeshen M; Department of Biology, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia., Khan TJ; Stem Cell P2 Laboratory, The Center for Reproductive Medicine, Shantou University Medical College, Shantou 515041, People's Republic of China., Khan KA; Chemistry Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia., Afifi M; Department of Biology, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia.; Biochemistry Department, Faculty of Veterinary Medicine, Zagazig University, Egypt., Al-Farga A; Department of Biochemistry, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia., Warsi MK; Department of Biochemistry, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia., Alkhaled M; Department of Biology, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia., Alayafi AAM; Department of Biology, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia.
Jazyk: angličtina
Zdroj: Royal Society open science [R Soc Open Sci] 2018 Nov 28; Vol. 5 (11), pp. 172164. Date of Electronic Publication: 2018 Nov 28 (Print Publication: 2018).
DOI: 10.1098/rsos.172164
Abstrakt: 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 enzyme lost just 28% of its initial activity. Owing to immobilization, the pH of the soluble α-amylase was shifted from 6.0 to 6.5. The immobilized α-amylases showed thermal stability at 60°C, and became more resistant to heavy metal ions. The k m values of the immobilized and soluble α-amylases were 9.6 and 3.8 mg starch ml -1 , respectively. In conclusion, this method shows that the immobilized α-amylase proved to be more efficient than its soluble form, and hence could be used during saccharification of starch.
Competing Interests: All authors declare no competing interests.
Databáze: MEDLINE
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