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Unfolded Lipase at Interfaces Studied via Interfacial Dilational Rheology: The Impact of Urea

Dowlati, Saeid ; Javadi, Aliyar ; Miller, Reinhard ; Eckert, Kerstin ; Kraume, Matthias (2022):
Unfolded Lipase at Interfaces Studied via Interfacial Dilational Rheology: The Impact of Urea. (Publisher's Version)
In: Colloids and Interfaces, 6 (4), MDPI, e-ISSN 2504-5377,
DOI: 10.26083/tuprints-00022835,
[Article]

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.

Item Type: Article
Erschienen: 2022
Creators: Dowlati, Saeid ; Javadi, Aliyar ; Miller, Reinhard ; Eckert, Kerstin ; Kraume, Matthias
Origin: Secondary publication DeepGreen
Status: Publisher's Version
Title: Unfolded Lipase at Interfaces Studied via Interfacial Dilational Rheology: The Impact of Urea
Language: English
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.

Journal or Publication Title: Colloids and Interfaces
Volume of the journal: 6
Issue Number: 4
Place of Publication: Darmstadt
Publisher: MDPI
Collation: 14 Seiten
Uncontrolled Keywords: lipase, protein unfolding, interfacial dilational rheology, interfacial viscoelasticity, profile analysis tensiometer, urea-induced unfolding
Divisions: 05 Department of Physics
05 Department of Physics > Institute for Condensed Matter Physics
05 Department of Physics > Institute for Condensed Matter Physics > Soft Matter Biophysics
Date Deposited: 07 Nov 2022 12:07
DOI: 10.26083/tuprints-00022835
URL / URN: https://tuprints.ulb.tu-darmstadt.de/22835
URN: urn:nbn:de:tuda-tuprints-228353
Additional Information:

This article belongs to the Special Issue Biocolloids and Biointerfaces

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