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. |
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| 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] |
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| Database: | Engineering Source |
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| 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] |
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| ISSN: | 18673880 |
| DOI: | 10.1002/cctc.202500038 |
