Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization

Molecules

Saleh A. Mohamed¹  Jalaluddin A. Khan¹  Omar A. M. Al-Bar¹ 

[1] Biochemistry Department, Faculty of Science, King Abdulaziz University, 21589, Jeddah, Kingdom of Saudi Arabia; E-Mails:

关键词: Trichoderma harzianum;    α-amylase;    immobilized enzyme;    optimization;   

DOI  :  10.3390/molecules19068027

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.