Cross-linked enzyme aggregates (CLEAs) and magnetic nanocomposite grafted CLEAs of GH26 endo-β-1,4-mannanase : Improved activity, stability and reusability
Copyright © 2017 Elsevier B.V. All rights reserved..
A comparative study on immobilization of recombinant endo-β-1,4-mannanase (ManB-1601), using cross-linked aggregated form (MB-C) and novel chitosan magnetic nanocomposites of MB-C (MB-Mag-C) was carried out. FT-IR and Raman spectroscopy were used to confirm the surface modifications while, scanning electron and atomic force microscopy were performed to demonstrate the surface topology and magnetic nature of MB-C and MB-Mag-C. Among MB-C and MB-Mag-C, the former showed better activity and stability in broad range of pH, thermo-stability and kinetic parameters while, the latter showed higher temperature optima and solvent stability. MB-C and MB-Mag-C when compared with free enzyme showed up to 73.2% higher activity (pH 4-9), up to 95.6% higher stability (pH 3-10, 9h incubation at room temperature), up to 15°C higher optimal temperature, higher stability (up to 83%) in the presence of solvents and up to 1.62-fold higher deactivation energy (Ed). Immobilized enzymes were able to repeatedly hydrolyze locust bean gum till 12 cycles and generated predominantly di-, tri- and tetra- species of β-manno-oligosaccharides.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2017 |
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Erschienen: |
2017 |
Enthalten in: |
Zur Gesamtaufnahme - volume:105 |
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Enthalten in: |
International journal of biological macromolecules - 105(2017), Pt 1 vom: 01. Dez., Seite 1289-1299 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Panwar, Deepesh [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 06.06.2018 Date Revised 06.06.2018 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.ijbiomac.2017.07.154 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM274422611 |
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500 | |a published: Print-Electronic | ||
500 | |a Citation Status MEDLINE | ||
520 | |a Copyright © 2017 Elsevier B.V. All rights reserved. | ||
520 | |a A comparative study on immobilization of recombinant endo-β-1,4-mannanase (ManB-1601), using cross-linked aggregated form (MB-C) and novel chitosan magnetic nanocomposites of MB-C (MB-Mag-C) was carried out. FT-IR and Raman spectroscopy were used to confirm the surface modifications while, scanning electron and atomic force microscopy were performed to demonstrate the surface topology and magnetic nature of MB-C and MB-Mag-C. Among MB-C and MB-Mag-C, the former showed better activity and stability in broad range of pH, thermo-stability and kinetic parameters while, the latter showed higher temperature optima and solvent stability. MB-C and MB-Mag-C when compared with free enzyme showed up to 73.2% higher activity (pH 4-9), up to 95.6% higher stability (pH 3-10, 9h incubation at room temperature), up to 15°C higher optimal temperature, higher stability (up to 83%) in the presence of solvents and up to 1.62-fold higher deactivation energy (Ed). Immobilized enzymes were able to repeatedly hydrolyze locust bean gum till 12 cycles and generated predominantly di-, tri- and tetra- species of β-manno-oligosaccharides | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Chitosan magnetic nanocomposites | |
650 | 4 | |a Cross-linked enzyme aggregates | |
650 | 4 | |a Endo-β-1,4-mannanase | |
650 | 4 | |a Thermal inactivation kinetics | |
650 | 4 | |a β-Manno-oligosaccharides | |
650 | 7 | |a Enzymes, Immobilized |2 NLM | |
650 | 7 | |a Oligosaccharides |2 NLM | |
650 | 7 | |a Protein Aggregates |2 NLM | |
650 | 7 | |a Chitosan |2 NLM | |
650 | 7 | |a 9012-76-4 |2 NLM | |
650 | 7 | |a Mannosidases |2 NLM | |
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650 | 7 | |a Mannose |2 NLM | |
650 | 7 | |a PHA4727WTP |2 NLM | |
700 | 1 | |a Kaira, Gaurav Singh |e verfasserin |4 aut | |
700 | 1 | |a Kapoor, Mukesh |e verfasserin |4 aut | |
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