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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.
In: Colloids and Interfaces, 2022, 6 (4)
doi: 10.26083/tuprints-00022835
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Item Type: Article
Type of entry: Secondary publication
Title: Unfolded Lipase at Interfaces Studied via Interfacial Dilational Rheology: The Impact of Urea
Language: English
Date: 7 November 2022
Place of Publication: Darmstadt
Year of primary publication: 2022
Publisher: MDPI
Journal or Publication Title: Colloids and Interfaces
Volume of the journal: 6
Issue Number: 4
Collation: 14 Seiten
DOI: 10.26083/tuprints-00022835
Corresponding Links:
Origin: Secondary publication DeepGreen

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.

Uncontrolled Keywords: lipase, protein unfolding, interfacial dilational rheology, interfacial viscoelasticity, profile analysis tensiometer, urea-induced unfolding
Status: Publisher's Version
URN: urn:nbn:de:tuda-tuprints-228353
Additional Information:

This article belongs to the Special Issue Biocolloids and Biointerfaces

Classification DDC: 500 Science and mathematics > 540 Chemistry
500 Science and mathematics > 570 Life sciences, biology
600 Technology, medicine, applied sciences > 620 Engineering and machine engineering
Divisions: 05 Department of Physics > Institute for Condensed Matter Physics > Soft Matter Biophysics
Date Deposited: 07 Nov 2022 12:07
Last Modified: 14 Nov 2023 19:05
SWORD Depositor: Deep Green
URI: https://tuprints.ulb.tu-darmstadt.de/id/eprint/22835
PPN: 501613617
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