The changing face of SDS denaturation: Complexes of Thermomyces lanuginosus lipase with SDS at pH 4.0, 6.0 and 8.0

Autor: Helena Østergaard Rasmussen, Daniel T. Weltz Wollenberg, Huabing Wang, Kell K. Andersen, Cristiano L.P. Oliveira, Christian Isak Jørgensen, Thomas J.D. Jørgensen, Daniel E. Otzen, Jan Skov Pedersen

Publikováno v: Rasmussen, H Ø, Wollenberg, D T W, Wang, H, Andersen, K K, Oliveira, C L P, Jørgensen, C I, Jørgensen, T J D, Otzen, D E & Pedersen, J S 2022, ' The changing face of SDS denaturation : Complexes of Thermomyces lanuginosus lipase with SDS at pH 4.0, 6.0 and 8.0 ', Journal of Colloid and Interface Science, vol. 614, pp. 214-232 . https://doi.org/10.1016/j.jcis.2021.12.188
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

HYPOTHESIS: Lipases are widely used in the detergent industry and must withstand harsh conditions involving both anionic and zwitterionic surfactants at alkaline pH. Thermomyces lanuginosus lipase (TlL) is often used and stays active at high concentr

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https://doi.org/10.1016/j.jcis.2021.12.188

Myoglobin and α-Lactalbumin Form Smaller Complexes with the Biosurfactant Rhamnolipid Than with SDS

Autor: Daniel E. Otzen, Thomas Vosegaard, Kell K. Andersen, Jan Skov Pedersen, G. Roshan Deen, Jens Kvist Madsen, Henriette Gavlshøj Mortensen

Publikováno v: Mortensen, H G, Madsen, J K, Andersen, K K, Vosegaard, T, Deen, G R, Otzen, D E & Pedersen, J S 2017, ' Myoglobin and α-Lactalbumin Form Smaller Complexes with the Biosurfactant Rhamnolipid Than with SDS ', Biophysical Journal, vol. 113, no. 12, pp. 2621-2633 . https://doi.org/10.1016/j.bpj.2017.10.024

Biosurfactants (BSs) attract increasing attention as sustainable alternatives to petroleum-derived surfactants. This necessitates structural insight into how BSs interact with proteins encountered by current chemical surfactants. Thus, small-angle x-

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https://doi.org/10.1016/j.bpj.2017.10.024

Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation

Autor: Tim Tolker-Nielsen, Gunna Christiansen, Kell K. Andersen, Daniel E. Otzen, Lars Kjær, Brian S. Vad

Publikováno v: Andersen, K K, Vad, B S, Kjaer, L, Tolker-Nielsen, T, Christiansen, G & Otzen, D E 2018, ' Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation ', FEBS Letters, vol. 592, no. 9, pp. 1484-1496 . https://doi.org/10.1002/1873-3468.13038

The Parkinson's disease-associated protein α-synuclein (αSN) is natively unfolded but its structure can be modulated by membranes and surfactants. The opportunistic pathogen Pseudomonas aeruginosa (PA) produces and secretes the biosurfactant rhamno

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https://pure.au.dk/portal/da/publications/pseudomonas-aeruginosa-rhamnolipid-induces-fibrillation-of-human-synuclein-and-modulates-its-effect-on-biofilm-formation(40d02970-b47b-4b98-b4c8-22811d2e0290).html

Human lysozyme peptidase resistance is perturbed by the anionic glycolipid biosurfactant rhamnolipid produced by the opportunistic pathogen Pseudomonas aeruginosa

Autor: Jan J. Enghild, Kell K. Andersen, Brian S. Vad, Carsten Scavenius, Daniel E. Otzen

Publikováno v: Andersen, K K, Vad, B S, Scavenius, C, Enghild, J J & Otzen, D E 2017, ' Human lysozyme peptidase resistance is perturbed by the anionic glycolipid biosurfactant rhamnolipid produced by the opportunistic pathogen Pseudomonas aeruginosa ', Biochemistry, vol. 56, no. 1, pp. 260–270 . https://doi.org/10.1021/acs.biochem.6b01009

Infection by the opportunistic pathogen Pseudomonas aeruginosa (PA) is accompanied by the secretion of virulence factors such as the secondary metabolite rhamnolipid (RL) as well as an array of bacterial enzymes, including the protease elastase. The

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https://pure.au.dk/portal/da/publications/human-lysozyme-peptidase-resistance-is-perturbed-by-the-anionic-glycolipid-biosurfactant-rhamnolipid-produced-by-the-opportunistic-pathogen-pseudomonas-aeruginosa(09ee6f4e-1916-4096-a8c7-9a44c2f07268).html

Stable intermediates determine proteins' primary unfolding sites in the presence of surfactants

Autor: Daniel E. Otzen, Jan J. Enghild, Steen V. Petersen, Jonas Høeg Hansen, Ture Damhus, Kell K. Andersen

Publikováno v: Petersen, S V, Andersen, K K, Enghild, J J, Damhus, T, Otzen, D & Hansen, J H 2009, ' Stable intermediates determine proteins' primary unfolding sites in the presence of surfactants ', Biopolymers, vol. 91, no. 3, pp. 221-231 .
Hansen, J H, Petersen, S V, Andersen, K K, Enghild, J J, Damhus, T & Otzen, D 2009, ' Stable intermediates determine proteins' primary unfolding sites in the presence of surfactants ', Biopolymers, vol. 91, no. 3, pp. 221-31 . https://doi.org/10.1002/bip.21125

Udgivelsesdato: 2009-Mar Despite detailed knowledge of the overall structural changes and stoichiometries of surfactant binding, little is known about which protein regions constitute the preferred sites of attack for initial unfolding. Here we have

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https://doi.org/10.1002/bip.21125