Optimal immobilization of ß -galactosidase onto -carrageenan gel beads using response surface methodology and its applications
|dc.contributor.author||Mohy Eldin, M.|
|dc.identifier.citation||Elnashar, M. and Awad, G. and Hassan, M. and Mohy Eldin, M. and Haroun, B. and El-Diwany, A. 2014. Optimal immobilization of ß -galactosidase onto -carrageenan gel beads using response surface methodology and its applications. The Scientific World Journal. 2014.|
ß-Galactosidase (ß-gal) was immobilized by covalent binding on novel -carrageenan gel beads activated by two-step method; the gel beads were soaked in polyethyleneimine followed by glutaraldehyde. 22 full-factorial central composite experiment designs were employed to optimize the conditions for the maximum enzyme loading efficiency. 11.443 U of enzyme/g gel beads was achieved by soaking 40 units of enzyme with the gel beads for eight hours. Immobilization process increased the pH from 4.5 to 5.5 and operational temperature from 50 to 55°C compared to the free enzyme. The apparent Km after immobilization was 61.6 mM compared to 22.9 mM for free enzyme. Maximum velocity Vmax was 131.2 mol·min-1 while it was 177.1 mol·min-1 for free enzyme. The full conversion experiment showed that the immobilized enzyme form is active as that of the free enzyme as both of them reached their maximum 100% relative hydrolysis at 4 h. The reusability test proved the durability of the -carrageenan beads loaded with ß-galactosidase for 20 cycles with retention of 60% of the immobilized enzyme activity to be more convenient for industrial uses. © 2014 Magdy M. Elnashar et al.
|dc.title||Optimal immobilization of ß -galactosidase onto -carrageenan gel beads using response surface methodology and its applications|
|dcterms.source.title||The Scientific World Journal|
|curtin.department||School of Biomedical Sciences|
|curtin.accessStatus||Open access via publisher|
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