Immobilization of Naringinase from <i>Aspergillus Niger</i> on a Magnetic Polysaccharide Carrier
Naringinase is an enzymatic complex used in the deglycosylation of compounds with a high application potential in the food and pharmaceutical industries. The aim of the study was to immobilize naringinase from <i>Aspergillus niger</i> KMS on a magnetic carrier obtained on the basis of ca...
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| Format: | Article |
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MDPI AG
2020-06-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/25/12/2731 |
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| author | Joanna Bodakowska-Boczniewicz Zbigniew Garncarek |
| author_facet | Joanna Bodakowska-Boczniewicz Zbigniew Garncarek |
| author_sort | Joanna Bodakowska-Boczniewicz |
| collection | DOAJ |
| description | Naringinase is an enzymatic complex used in the deglycosylation of compounds with a high application potential in the food and pharmaceutical industries. The aim of the study was to immobilize naringinase from <i>Aspergillus niger</i> KMS on a magnetic carrier obtained on the basis of carob gum activated by polyethyleneimine. Response surface methodology was used to optimize naringinase immobilization taking into account the following factors: pH, immobilization time, initial concentration of naringinase and immobilization temperature. The adsorption of the enzyme on a magnetic carrier was a reversible process. The binding force of naringinase was increased by crosslinking the enzyme with the carrier using dextran aldehyde. The crosslinked enzyme had better stability in an acidic environment and at a higher temperature compared to the free form. The immobilization and stabilization of naringinase by dextran aldehyde on the magnetic polysaccharide carrier lowered the activation energy, thus increasing the catalytic capacity of the investigated enzyme and increasing the activation energy of the thermal deactivation process, which confirms higher stability of the immobilized enzyme in comparison with free naringinase. The preparation of crosslinked naringinase retained over 80% of its initial activity after 10 runs of naringin hydrolysis from fresh and model grapefruit juice. |
| first_indexed | 2024-03-10T19:13:12Z |
| format | Article |
| id | doaj.art-95f16020bf6e4de8935f823847e89336 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T19:13:12Z |
| publishDate | 2020-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-95f16020bf6e4de8935f823847e893362023-11-20T03:38:04ZengMDPI AGMolecules1420-30492020-06-012512273110.3390/molecules25122731Immobilization of Naringinase from <i>Aspergillus Niger</i> on a Magnetic Polysaccharide CarrierJoanna Bodakowska-Boczniewicz0Zbigniew Garncarek1Department of Biotechnology and Food Analysis, Wroclaw University of Economics and Business, 53–345 Wroclaw, PolandDepartment of Biotechnology and Food Analysis, Wroclaw University of Economics and Business, 53–345 Wroclaw, PolandNaringinase is an enzymatic complex used in the deglycosylation of compounds with a high application potential in the food and pharmaceutical industries. The aim of the study was to immobilize naringinase from <i>Aspergillus niger</i> KMS on a magnetic carrier obtained on the basis of carob gum activated by polyethyleneimine. Response surface methodology was used to optimize naringinase immobilization taking into account the following factors: pH, immobilization time, initial concentration of naringinase and immobilization temperature. The adsorption of the enzyme on a magnetic carrier was a reversible process. The binding force of naringinase was increased by crosslinking the enzyme with the carrier using dextran aldehyde. The crosslinked enzyme had better stability in an acidic environment and at a higher temperature compared to the free form. The immobilization and stabilization of naringinase by dextran aldehyde on the magnetic polysaccharide carrier lowered the activation energy, thus increasing the catalytic capacity of the investigated enzyme and increasing the activation energy of the thermal deactivation process, which confirms higher stability of the immobilized enzyme in comparison with free naringinase. The preparation of crosslinked naringinase retained over 80% of its initial activity after 10 runs of naringin hydrolysis from fresh and model grapefruit juice.https://www.mdpi.com/1420-3049/25/12/2731naringinaseimmobilizationmagnetic carrierdextran aldehyde |
| spellingShingle | Joanna Bodakowska-Boczniewicz Zbigniew Garncarek Immobilization of Naringinase from <i>Aspergillus Niger</i> on a Magnetic Polysaccharide Carrier Molecules naringinase immobilization magnetic carrier dextran aldehyde |
| title | Immobilization of Naringinase from <i>Aspergillus Niger</i> on a Magnetic Polysaccharide Carrier |
| title_full | Immobilization of Naringinase from <i>Aspergillus Niger</i> on a Magnetic Polysaccharide Carrier |
| title_fullStr | Immobilization of Naringinase from <i>Aspergillus Niger</i> on a Magnetic Polysaccharide Carrier |
| title_full_unstemmed | Immobilization of Naringinase from <i>Aspergillus Niger</i> on a Magnetic Polysaccharide Carrier |
| title_short | Immobilization of Naringinase from <i>Aspergillus Niger</i> on a Magnetic Polysaccharide Carrier |
| title_sort | immobilization of naringinase from i aspergillus niger i on a magnetic polysaccharide carrier |
| topic | naringinase immobilization magnetic carrier dextran aldehyde |
| url | https://www.mdpi.com/1420-3049/25/12/2731 |
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