Title
Characterization and analysis of the adsorption immobilization mechanism of <tex>$\beta$</tex>-galactosidase on metal oxide powders Characterization and analysis of the adsorption immobilization mechanism of <tex>$\beta$</tex>-galactosidase on metal oxide powders
Author
Faculty/Department
Faculty of Sciences. Chemistry
Publication type
article
Publication
Subject
Chemistry
Source (journal)
RSC advances
Volume/pages
3(2013) :46 , p. 24054-24062
ISSN
2046-2069
ISI
000326745100030
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
Immobilization of the enzymes plays a vital role in enhancing their applicability in a wide range of applications, thus ensuring the use of sustainable enzymatic processes over the conventional chemical processes on an industrial scale. This study provides the background information for the selection and screening of inorganic metal oxide (MO) powders for their use as fillers in mixed matrix membranes for enzyme immobilization as the future aim. A total of 13 MOs, ranging in size from 0.01 μm to <5 μm, were tested for their performance as a support for enzyme (β-galactosidase) immobilization via adsorption. Alumina appeared to be the best performing MO with the amount and activity of the immobilized enzyme being 64 mg g−1 and up to 288 U g−1, respectively. The amount of immobilized enzyme on alumina (α-Al2O3 C and γ-Al2O3) was >3 times higher than ZrO2 (used as a reference MO in this study). Upon heat treatment at 900 °C, up to 15%, 52% and 42% decline was observed in the amount of immobilized enzyme in case of alumina metal oxides (MOs), ZrO2 and TiO2, respectively. The results suggested that both isoelectric point and surface area of the MO influence the immobilization. The most important observation in this study was that the bonding of the enzyme to the MO surface seems to be mediated by the bonding/interaction of the buffer to the enzyme.
E-info
https://repository.uantwerpen.be/docman/iruaauth/dd80f0/8774d5e33c9.pdf
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