Dowlati, Saeid ; Javadi, Aliyar ; Miller, Reinhard ; Eckert, Kerstin ; Kraume, Matthias (2022)
Unfolded Lipase at Interfaces Studied via Interfacial Dilational Rheology: The Impact of Urea.
In: Colloids and Interfaces, 6 (4)
doi: 10.3390/colloids6040056
Artikel, Bibliographie
Dies ist die neueste Version dieses Eintrags.
Kurzbeschreibung (Abstract)
Unfolding can interrupt the activity of enzymes. Lipase, the enzyme responsible for triglyceride catalysis, can be deactivated by unfolding, which can significantly affect the yield of enzymatic processes in biochemical engineering. Different agents can induce lipase unfolding, among which we study the impact of urea as a strong denaturant. Unfolding weakens the rigidity and stability of globular proteins, thereby changing the viscoelastic properties of the protein adsorbed layers. These changes can be detected and quantified using interfacial dilational rheology. The urea-induced unfolding of lipase destructs its globular structure, making it more flexible. The interfacial tension and viscoelastic moduli of lipase adsorbed layers reduce upon the addition of urea in the range of studied concentrations. The results agree with the theory that, upon unfolding, a distal region of the loop and tail domain forms adjacent to the proximal region of the interface. The exchange of matter between these regions reduces the viscoelasticity of the unfolded lipase adsorbed layers. Additionally, unfolding reduces the rigidity and brittleness of the lipase adsorbed layers: the aged adsorbed layer of native lipase can break upon high-amplitude perturbations of the interfacial area, unlike the case for urea-induced unfolded lipase.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2022 |
| Autor(en): | Dowlati, Saeid ; Javadi, Aliyar ; Miller, Reinhard ; Eckert, Kerstin ; Kraume, Matthias |
| Art des Eintrags: | Bibliographie |
| Titel: | Unfolded Lipase at Interfaces Studied via Interfacial Dilational Rheology: The Impact of Urea |
| Sprache: | Englisch |
| Publikationsjahr: | 2022 |
| Ort: | Darmstadt |
| Verlag: | MDPI |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Colloids and Interfaces |
| Jahrgang/Volume einer Zeitschrift: | 6 |
| (Heft-)Nummer: | 4 |
| Kollation: | 14 Seiten |
| DOI: | 10.3390/colloids6040056 |
| Zugehörige Links: | |
| Kurzbeschreibung (Abstract): | Unfolding can interrupt the activity of enzymes. Lipase, the enzyme responsible for triglyceride catalysis, can be deactivated by unfolding, which can significantly affect the yield of enzymatic processes in biochemical engineering. Different agents can induce lipase unfolding, among which we study the impact of urea as a strong denaturant. Unfolding weakens the rigidity and stability of globular proteins, thereby changing the viscoelastic properties of the protein adsorbed layers. These changes can be detected and quantified using interfacial dilational rheology. The urea-induced unfolding of lipase destructs its globular structure, making it more flexible. The interfacial tension and viscoelastic moduli of lipase adsorbed layers reduce upon the addition of urea in the range of studied concentrations. The results agree with the theory that, upon unfolding, a distal region of the loop and tail domain forms adjacent to the proximal region of the interface. The exchange of matter between these regions reduces the viscoelasticity of the unfolded lipase adsorbed layers. Additionally, unfolding reduces the rigidity and brittleness of the lipase adsorbed layers: the aged adsorbed layer of native lipase can break upon high-amplitude perturbations of the interfacial area, unlike the case for urea-induced unfolded lipase. |
| Freie Schlagworte: | lipase, protein unfolding, interfacial dilational rheology, interfacial viscoelasticity, profile analysis tensiometer, urea-induced unfolding |
| Zusätzliche Informationen: | This article belongs to the Special Issue Biocolloids and Biointerfaces |
| Sachgruppe der Dewey Dezimalklassifikatin (DDC): | 500 Naturwissenschaften und Mathematik > 540 Chemie 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie 600 Technik, Medizin, angewandte Wissenschaften > 620 Ingenieurwissenschaften und Maschinenbau |
| Fachbereich(e)/-gebiet(e): | 05 Fachbereich Physik 05 Fachbereich Physik > Institut für Physik Kondensierter Materie (IPKM) 05 Fachbereich Physik > Institut für Physik Kondensierter Materie (IPKM) > Physik biologischer weicher Materie |
| Hinterlegungsdatum: | 02 Aug 2024 12:44 |
| Letzte Änderung: | 02 Aug 2024 12:44 |
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| Suche nach Titel in: | TUfind oder in Google |
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Unfolded Lipase at Interfaces Studied via Interfacial Dilational Rheology: The Impact of Urea. (deposited 07 Nov 2022 12:07)
- Unfolded Lipase at Interfaces Studied via Interfacial Dilational Rheology: The Impact of Urea. (deposited 02 Aug 2024 12:44) [Gegenwärtig angezeigt]
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