Exposure Experiments to Test the Kinetic Stability of 5‐Hydroxymethylfurfural Oxidase (HMFO) in Different Reactor Environments.

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Title: Exposure Experiments to Test the Kinetic Stability of 5‐Hydroxymethylfurfural Oxidase (HMFO) in Different Reactor Environments.
Authors: Høst, Amalie Vang1,2 (AUTHOR), Meyer, Moritz3 (AUTHOR), Bongratz, Patrick3 (AUTHOR), Fraaije, Marco W.4 (AUTHOR), Woodley, John M.1 (AUTHOR) jw@kt.dtu.dk
Source: ChemCatChem. 7/8/2025, Vol. 17 Issue 13, p1-11. 11p.
Subjects: Gas-liquid interfaces, Enzyme inactivation, Cavitation, Hydroxymethylfurfural, Electric reactors, Turbulence, Denaturation of proteins, Dynamic stability
Abstract: The impact of agitation on protein aggregation is often misattributed to shear stress rather than related phenomena such as cavitation and gas entrainment from the surface. For some time now, it has been known that shear is unlikely to harm most proteins directly. Rather, interfacial phenomena, particularly those involving dynamic gas‐liquid interfaces are critical contributors to protein damage, which leads to aggregation and compromises stability. This work investigated the kinetic stability of 5‐hydroxymethylfurfural oxidase (HMFO; EC: 1.1.3.47) in a 2 L stirred tank reactor. Exposure experiments revealed that the leading cause of enzyme deactivation was exposure to the gas‐liquid interface, either produced deliberately when sparging gas into the system or by accidental air entrainment from the overhead space due to mechanical stirring. This was further proven by experiments using the Bio Thrust membrane module, which enabled bubble‐free aeration thus, confirming that exposure to the gas‐liquid interface is the leading cause of deactivation. [ABSTRACT FROM AUTHOR]
Copyright of ChemCatChem is the property of Wiley-Blackwell 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.)
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  Data: Exposure Experiments to Test the Kinetic Stability of 5‐Hydroxymethylfurfural Oxidase (HMFO) in Different Reactor Environments.
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  Data: <searchLink fieldCode="JN" term="%22ChemCatChem%22">ChemCatChem</searchLink>. 7/8/2025, Vol. 17 Issue 13, p1-11. 11p.
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  Data: <searchLink fieldCode="DE" term="%22Gas-liquid+interfaces%22">Gas-liquid interfaces</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+inactivation%22">Enzyme inactivation</searchLink><br /><searchLink fieldCode="DE" term="%22Cavitation%22">Cavitation</searchLink><br /><searchLink fieldCode="DE" term="%22Hydroxymethylfurfural%22">Hydroxymethylfurfural</searchLink><br /><searchLink fieldCode="DE" term="%22Electric+reactors%22">Electric reactors</searchLink><br /><searchLink fieldCode="DE" term="%22Turbulence%22">Turbulence</searchLink><br /><searchLink fieldCode="DE" term="%22Denaturation+of+proteins%22">Denaturation of proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Dynamic+stability%22">Dynamic stability</searchLink>
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  Data: The impact of agitation on protein aggregation is often misattributed to shear stress rather than related phenomena such as cavitation and gas entrainment from the surface. For some time now, it has been known that shear is unlikely to harm most proteins directly. Rather, interfacial phenomena, particularly those involving dynamic gas‐liquid interfaces are critical contributors to protein damage, which leads to aggregation and compromises stability. This work investigated the kinetic stability of 5‐hydroxymethylfurfural oxidase (HMFO; EC: 1.1.3.47) in a 2 L stirred tank reactor. Exposure experiments revealed that the leading cause of enzyme deactivation was exposure to the gas‐liquid interface, either produced deliberately when sparging gas into the system or by accidental air entrainment from the overhead space due to mechanical stirring. This was further proven by experiments using the Bio Thrust membrane module, which enabled bubble‐free aeration thus, confirming that exposure to the gas‐liquid interface is the leading cause of deactivation. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of ChemCatChem is the property of Wiley-Blackwell 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: 10.1002/cctc.202500038
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      – Code: eng
        Text: English
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        PageCount: 11
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      – SubjectFull: Gas-liquid interfaces
        Type: general
      – SubjectFull: Enzyme inactivation
        Type: general
      – SubjectFull: Cavitation
        Type: general
      – SubjectFull: Hydroxymethylfurfural
        Type: general
      – SubjectFull: Electric reactors
        Type: general
      – SubjectFull: Turbulence
        Type: general
      – SubjectFull: Denaturation of proteins
        Type: general
      – SubjectFull: Dynamic stability
        Type: general
    Titles:
      – TitleFull: Exposure Experiments to Test the Kinetic Stability of 5‐Hydroxymethylfurfural Oxidase (HMFO) in Different Reactor Environments.
        Type: main
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          Name:
            NameFull: Høst, Amalie Vang
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            NameFull: Meyer, Moritz
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            NameFull: Fraaije, Marco W.
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            NameFull: Woodley, John M.
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              M: 07
              Text: 7/8/2025
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              Y: 2025
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