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Immobilization of soybean peroxidase on aminopropyl glass beads: Structural and kinetic studies

Paper ID Volume ID Publish Year Pages File Format Full-Text
3500 173 2012 7 PDF Available
Title
Immobilization of soybean peroxidase on aminopropyl glass beads: Structural and kinetic studies
Abstract

The enzyme soybean peroxidase (SBP) is able to catalyze the oxidation of a large number of substrates and is characterized by high resistance to both chemical and thermal denaturation. In this contribution SBP was covalently immobilized on aminopropyl glass beads (APG) in order to obtain a solid biocatalyst, useful either in degradation of pollutants or in specific oxidative reactions. Several samples of immobilized SBP were first synthesized and then characterized by means of some experimental techniques (FT-IR, ESR, and UV–visible spectroscopies, gas-volumetric adsorption of nitrogen at 77 K, SEM). Moreover, different kinetic measurements were carried out to determine activity and stability properties of these biocatalysts. Our data indicate that (i) the SBP catalytic site was partially modified during the immobilization process, but the enzyme retained about 35% of its specific activity after immobilization, and (ii) the biocatalyst exhibits a significant improvement of SBP stability over time, preserving up to 50% of its initial activity after 70 days of storage and 85% when used in ten consecutive reaction cycles.

Graphical abstract.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► We immobilized soybean peroxidase (SBP) on aminopropyl glass beads. ► The system was characterized by different spectroscopic techniques. ► The immobilization process slightly modify the Fe(III)-heme catalytic site of SBP. ► The system retain a good percentage of catalytic activity and resist to storage.

Keywords
Immobilization; Immobilized enzymes; Heterogenous biocatalysis; Enzyme activity; Soybean; Peroxidase
First Page Preview
Immobilization of soybean peroxidase on aminopropyl glass beads: Structural and kinetic studies
Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 67, 15 August 2012, Pages 28–34
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering