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

Autor: Aisha A. M. Alayafi, Yaaser Q. Almulaiky, Mohiuddin Khan Warsi, Musab Aldhahri, Mohammed N. Baeshen, Mohammed Alkhaled, Tariq Jamal Khan, Mohamed Afifi, Ammar AL-Farga, Khalid A. Khan, Faisal M. Aqlan
Jazyk: angličtina
Rok vydání: 2018
Předmět:
Zdroj: Royal Society Open Science, Vol 5, Iss 11 (2018)
Royal Society Open Science
ISSN: 2054-5703
DOI: 10.1098/rsos.172164
Popis: 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.
Databáze: OpenAIRE