Autor: |
Saleh A. Mohamed, Jalaluddin A. Khan, Omar A. M. Al-Bar, Reda M. El-Shishtawy |
Jazyk: |
angličtina |
Rok vydání: |
2014 |
Předmět: |
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Zdroj: |
Molecules, Vol 19, Iss 6, Pp 8027-8038 (2014) |
Druh dokumentu: |
article |
ISSN: |
1420-3049 |
DOI: |
10.3390/molecules19068027 |
Popis: |
α-Amylase from Trichoderma harzianum was covalently immobilized on activated wool by cyanuric chloride. Immobilized α-amylase exhibited 75% of its initial activity after 10 runs. The soluble and immobilized α-amylases exhibited maximum activity at pH values 6.0 and 6.5, respectively. The immobilized enzyme was more thermally stable than the soluble one. Various substrates were hydrolyzed by immobilized α-amylase with high efficiencies compared to those of soluble α-amylase. The inhibition of the immobilized α-amylase by metal ions was low as compared with soluble enzyme. On the basis of the results obtained, immobilized α-amylase could be employed in the saccharification of starch processing. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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