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Active site titration of immobilized beta-galactosidase for the determination of active enzymes

Paper ID Volume ID Publish Year Pages File Format Full-Text
3084 149 2015 5 PDF Available
Title
Active site titration of immobilized beta-galactosidase for the determination of active enzymes
Abstract

•A quantitative active site titration method is described.•This method is effective for determining the amount of immobilized β-galactosidase of K. lactis on beads.•8.3 mg of active enzyme was found on 1 g of dried SPRIN imibond galactosidase beads.

In the present study, an active site titration method is demonstrated, to determine the amount of active enzyme (β-galactosidase), immobilized on a support. Two types of supports were investigated, viz. amino acrylic resin and a mixed matrix membrane. Furthermore, 2′,4′-dinitrophenyl 2-deoxy-2-fluoro-β-d-galactopyranoside was used as an inhibitor for the active site titration of immobilized β-galactosidase obtained from Kluyveromyces lactis. Using the active site titration, approximately 8.3 mg of active enzyme was found on 1 g of dried commercially available SPRIN imibond, which is an amino acrylic resin with covalently bound β-galactosidase obtained from K. lactis. However, this method, in its present form, was not effective on the mixed matrix membranes due to the irreversible partial adsorption of the leaving group (2′,4′-dinitrophenolate) by the membrane. This observation implied that it is important to investigate interactions between the support and the used inhibitor and leaving group.

Keywords
Active site titration; Enzyme; Beta-galactosidase; Immobilization; Beads; Membrane
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Active site titration of immobilized beta-galactosidase for the determination of active enzymes
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 93, 15 January 2015, Pages 137–141
Authors
, , , , , ,
Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
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Price after discount Only $4.95
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Full-text PDF Download
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