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A Health-Friendly Strategy for Covalent-Bonded Immobilization of Pectinase on the Functionalized Glass Beads
In recent years, polyaldehyde polysaccharides have received an increasing attention as an ideal cross-linker which their aldehyde groups can be crosslinked with amino groups of enzyme. In this study, pectinase was covalently immobilized on the glass beads by polyaldehyde pullulan as the resulting pr...
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Published in: | Food and bioprocess technology 2021, Vol.14 (1), p.177-186 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | In recent years, polyaldehyde polysaccharides have received an increasing attention as an ideal cross-linker which their aldehyde groups can be crosslinked with amino groups of enzyme. In this study, pectinase was covalently immobilized on the glass beads by polyaldehyde pullulan as the resulting product from periodate oxidation of this polysaccharide and by glutaraldehyde as a common cross-linker. Polyaldehyde pullulan had an aldehyde content of 19.9 ± 1.3%, which was confirmed by FTIR. The protein content of glass beads after enzyme immobilization by polyaldehyde pullulan and glutaraldehyde was 1.83 and 0.41 mg/10 glass beads, respectively. Optimum pH and temperature for pectinase immobilized by both cross-linkers were 5.5 and 50 °C, and the specific activity under these conditions was 2.21 ± 0.18 and 2.56 ± 0.12 unit/mg for enzyme immobilized by polyaldehyde pullulan and glutaraldehyde, respectively. pH stability of the pectinase immobilized by polyaldehyde pullulan was higher than by glutaraldehyde, while both immobilized system has an almost similar temperature stability. The kinetic parameters were determined for both immobilization systems. Also, SEM and atomic force microscopy confirmed the presence of polyaldehyde pullulan on glass bead after immobilization. Eventually, the obtained results suggested that polyaldehyde pullulan can be applied as a high potential alternative to glutaraldehyde for the enzyme immobilization. |
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ISSN: | 1935-5130 1935-5149 |
DOI: | 10.1007/s11947-020-02524-8 |