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Horseradish peroxidase immobilised onto electrospun fibres and its application in decolourisation of dyes from model sea water.

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Title: Horseradish peroxidase immobilised onto electrospun fibres and its application in decolourisation of dyes from model sea water.
Authors: Jankowska, Katarzyna1 (AUTHOR), Zdarta, Jakub1 (AUTHOR), Grzywaczyk, Adam1 (AUTHOR), Degórska, Oliwia1 (AUTHOR), Kijeńska-Gawrońska, Ewa2 (AUTHOR), Pinelo, Manuel3 (AUTHOR), Jesionowski, Teofil1 (AUTHOR) Teofil.Jesionowski@put.poznan.pl
Source: Process Biochemistry. Mar2021, Vol. 102, p10-21. 12p.
Subjects: Horseradish peroxidase, Seawater, Malachite green, Glutaraldehyde, Dyes & dyeing, Fibers
Abstract: • Polyamide 6 electrospun material was fabricated and characterised. • The horseradish immobilisation by adsorption and covalent binding was carried out. • The most efficient immobilisation conditions were: pH 7, 50 °C and 60 min of process. • The removal efficiencies were over 70% of Reactive Black 5 and 83% of Malachite Green. Despite many studies concerning dyes decolourisation, we propose a novel, cheap, eco-friendly and sustainable solution for highly effective dyes removal based on electrospun materials and immobilised enzyme. Our study provides proof-of-concept for the immobilisation of horseradish peroxidase (HRP) on polyamide 6 electrospun fibres by adsorption and covalent binding, and application for dyes decolourisation from imitating polluted sea waters. The highest relative activity of immobilised HRP was obtained after immobilisation performed at 50 °C and pH 7 for 60 min for adsorption method, as well as using 3% of glutaraldehyde concentration, 70 min of process time, 60 °C and pH 7 for covalent binding. Biocatalytic systems produced were found to possess high catalytic properties and were used for decolourisation of Reactive Black 5 and Malachite Green textile dyes from solutions imitating polluted sea waters, that is a novel approach for removal of pollutants from aqueous solutions. The highest decolourisation efficiencies of dyes were obtained after 60 min of treatment at pH 7 and temperature 25 °C and reached over 70%. In the future, the presented approach based on use of enzymes immobilised in decolourisation processes, might play significant role in industrial removal of dyes. [ABSTRACT FROM AUTHOR]
Copyright of Process Biochemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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DbLabel: Engineering Source
An: 148884803
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PubType: Academic Journal
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Items – Name: Title
  Label: Title
  Group: Ti
  Data: Horseradish peroxidase immobilised onto electrospun fibres and its application in decolourisation of dyes from model sea water.
– Name: Author
  Label: Authors
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  Data: <searchLink fieldCode="AR" term="%22Jankowska%2C+Katarzyna%22">Jankowska, Katarzyna</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zdarta%2C+Jakub%22">Zdarta, Jakub</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Grzywaczyk%2C+Adam%22">Grzywaczyk, Adam</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Degórska%2C+Oliwia%22">Degórska, Oliwia</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Kijeńska-Gawrońska%2C+Ewa%22">Kijeńska-Gawrońska, Ewa</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Pinelo%2C+Manuel%22">Pinelo, Manuel</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Jesionowski%2C+Teofil%22">Jesionowski, Teofil</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> Teofil.Jesionowski@put.poznan.pl</i>
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  Data: <searchLink fieldCode="JN" term="%22Process+Biochemistry%22">Process Biochemistry</searchLink>. Mar2021, Vol. 102, p10-21. 12p.
– Name: Subject
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  Data: <searchLink fieldCode="DE" term="%22Horseradish+peroxidase%22">Horseradish peroxidase</searchLink><br /><searchLink fieldCode="DE" term="%22Seawater%22">Seawater</searchLink><br /><searchLink fieldCode="DE" term="%22Malachite+green%22">Malachite green</searchLink><br /><searchLink fieldCode="DE" term="%22Glutaraldehyde%22">Glutaraldehyde</searchLink><br /><searchLink fieldCode="DE" term="%22Dyes+%26+dyeing%22">Dyes & dyeing</searchLink><br /><searchLink fieldCode="DE" term="%22Fibers%22">Fibers</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: • Polyamide 6 electrospun material was fabricated and characterised. • The horseradish immobilisation by adsorption and covalent binding was carried out. • The most efficient immobilisation conditions were: pH 7, 50 °C and 60 min of process. • The removal efficiencies were over 70% of Reactive Black 5 and 83% of Malachite Green. Despite many studies concerning dyes decolourisation, we propose a novel, cheap, eco-friendly and sustainable solution for highly effective dyes removal based on electrospun materials and immobilised enzyme. Our study provides proof-of-concept for the immobilisation of horseradish peroxidase (HRP) on polyamide 6 electrospun fibres by adsorption and covalent binding, and application for dyes decolourisation from imitating polluted sea waters. The highest relative activity of immobilised HRP was obtained after immobilisation performed at 50 °C and pH 7 for 60 min for adsorption method, as well as using 3% of glutaraldehyde concentration, 70 min of process time, 60 °C and pH 7 for covalent binding. Biocatalytic systems produced were found to possess high catalytic properties and were used for decolourisation of Reactive Black 5 and Malachite Green textile dyes from solutions imitating polluted sea waters, that is a novel approach for removal of pollutants from aqueous solutions. The highest decolourisation efficiencies of dyes were obtained after 60 min of treatment at pH 7 and temperature 25 °C and reached over 70%. In the future, the presented approach based on use of enzymes immobilised in decolourisation processes, might play significant role in industrial removal of dyes. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Process Biochemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
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      – Type: doi
        Value: 10.1016/j.procbio.2020.11.015
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      – Code: eng
        Text: English
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      Pagination:
        PageCount: 12
        StartPage: 10
    Subjects:
      – SubjectFull: Horseradish peroxidase
        Type: general
      – SubjectFull: Seawater
        Type: general
      – SubjectFull: Malachite green
        Type: general
      – SubjectFull: Glutaraldehyde
        Type: general
      – SubjectFull: Dyes & dyeing
        Type: general
      – SubjectFull: Fibers
        Type: general
    Titles:
      – TitleFull: Horseradish peroxidase immobilised onto electrospun fibres and its application in decolourisation of dyes from model sea water.
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            NameFull: Jankowska, Katarzyna
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            NameFull: Zdarta, Jakub
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            NameFull: Degórska, Oliwia
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            NameFull: Kijeńska-Gawrońska, Ewa
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            – D: 01
              M: 03
              Text: Mar2021
              Type: published
              Y: 2021
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              Value: 102
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