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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
Optimal immobilization of β -galactosidase onto -carrageenan gel beads using response surface methodology and its applications
The Scientific World Journal, Volume 2014, Article 571682, Year 2014
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Description
β-Galactosidase (β-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 β-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.
Authors & Co-Authors
Elnashar, Magdy M.
Egypt, Giza
National Research Centre
Awad, Ghada A.
Egypt, Giza
National Research Centre
Hassan, Mohamed E.
Egypt, Giza
National Research Centre
Mohy-Eldin, Mohamed S.
Egypt, New Borg el Arab
City of Scientific Research and Technological Applications
Haroun, Bakry M.
Egypt, Cairo
Faculty of Science
I. El-Diwany A., Ahmed I.
Egypt, Giza
National Research Centre
Statistics
Citations: 26
Authors: 6
Affiliations: 3
Identifiers
Doi:
10.1155/2014/571682
e-ISSN:
1537744X
Study Approach
Quantitative