Ionic strength-dependent denaturation of Thermomyces lanuginosus lipase induced by SDS

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Ionic strength-dependent denaturation of Thermomyces lanuginosus lipase induced by SDS. / Fanø, Mathias; van de Weert, Marco; Møller, Eva Horn; Kruse, Nanna Aaby; Frøkjær, Sven.

In: Archives of Biochemistry and Biophysics, Vol. 506, No. 1, 2011, p. 92-98.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Fanø, M, van de Weert, M, Møller, EH, Kruse, NA & Frøkjær, S 2011, 'Ionic strength-dependent denaturation of Thermomyces lanuginosus lipase induced by SDS', Archives of Biochemistry and Biophysics, vol. 506, no. 1, pp. 92-98. https://doi.org/10.1016/j.abb.2010.11.012

APA

Fanø, M., van de Weert, M., Møller, E. H., Kruse, N. A., & Frøkjær, S. (2011). Ionic strength-dependent denaturation of Thermomyces lanuginosus lipase induced by SDS. Archives of Biochemistry and Biophysics, 506(1), 92-98. https://doi.org/10.1016/j.abb.2010.11.012

Vancouver

Fanø M, van de Weert M, Møller EH, Kruse NA, Frøkjær S. Ionic strength-dependent denaturation of Thermomyces lanuginosus lipase induced by SDS. Archives of Biochemistry and Biophysics. 2011;506(1):92-98. https://doi.org/10.1016/j.abb.2010.11.012

Author

Fanø, Mathias ; van de Weert, Marco ; Møller, Eva Horn ; Kruse, Nanna Aaby ; Frøkjær, Sven. / Ionic strength-dependent denaturation of Thermomyces lanuginosus lipase induced by SDS. In: Archives of Biochemistry and Biophysics. 2011 ; Vol. 506, No. 1. pp. 92-98.

Bibtex

@article{5b4668ed30a54f78951dc39c7bcf40d1,
title = "Ionic strength-dependent denaturation of Thermomyces lanuginosus lipase induced by SDS",
abstract = "Triglyceride lipase from Thermomyces lanuginosus (TlL) has been reported to be resistant to denaturation by sodium dodecyl sulfate (SDS). We have found that at neutral pH, structural integrity is strongly dependent on ionic strength. In 10 mM phosphate buffer and SDS, the lipase exhibits a far-UV CD spectrum similar to other proteins denatured in this surfactant while the near-UV CD spectrum shows a complete loss of tertiary structure, observations supported by steady state fluorescence spectroscopy. However, when increasing the ionic strength by the addition of NaCl, the lipase was rendered resistant towards SDS denaturation, as observed by all techniques employed. The effect of salt on the critical micelle concentration (CMC) of SDS was observed to correlate with the effect on the degree of SDS-induced denaturation. This finding is compatible with the notion that the concentration of SDS monomers is a crucial factor for SDS–lipase interactions. The presented results are important for the understanding and improvement of protein stability in surfactant systems.",
keywords = "Former Faculty of Pharmaceutical Sciences",
author = "Mathias Fan{\o} and {van de Weert}, Marco and M{\o}ller, {Eva Horn} and Kruse, {Nanna Aaby} and Sven Fr{\o}kj{\ae}r",
year = "2011",
doi = "10.1016/j.abb.2010.11.012",
language = "English",
volume = "506",
pages = "92--98",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press",
number = "1",

}

RIS

TY - JOUR

T1 - Ionic strength-dependent denaturation of Thermomyces lanuginosus lipase induced by SDS

AU - Fanø, Mathias

AU - van de Weert, Marco

AU - Møller, Eva Horn

AU - Kruse, Nanna Aaby

AU - Frøkjær, Sven

PY - 2011

Y1 - 2011

N2 - Triglyceride lipase from Thermomyces lanuginosus (TlL) has been reported to be resistant to denaturation by sodium dodecyl sulfate (SDS). We have found that at neutral pH, structural integrity is strongly dependent on ionic strength. In 10 mM phosphate buffer and SDS, the lipase exhibits a far-UV CD spectrum similar to other proteins denatured in this surfactant while the near-UV CD spectrum shows a complete loss of tertiary structure, observations supported by steady state fluorescence spectroscopy. However, when increasing the ionic strength by the addition of NaCl, the lipase was rendered resistant towards SDS denaturation, as observed by all techniques employed. The effect of salt on the critical micelle concentration (CMC) of SDS was observed to correlate with the effect on the degree of SDS-induced denaturation. This finding is compatible with the notion that the concentration of SDS monomers is a crucial factor for SDS–lipase interactions. The presented results are important for the understanding and improvement of protein stability in surfactant systems.

AB - Triglyceride lipase from Thermomyces lanuginosus (TlL) has been reported to be resistant to denaturation by sodium dodecyl sulfate (SDS). We have found that at neutral pH, structural integrity is strongly dependent on ionic strength. In 10 mM phosphate buffer and SDS, the lipase exhibits a far-UV CD spectrum similar to other proteins denatured in this surfactant while the near-UV CD spectrum shows a complete loss of tertiary structure, observations supported by steady state fluorescence spectroscopy. However, when increasing the ionic strength by the addition of NaCl, the lipase was rendered resistant towards SDS denaturation, as observed by all techniques employed. The effect of salt on the critical micelle concentration (CMC) of SDS was observed to correlate with the effect on the degree of SDS-induced denaturation. This finding is compatible with the notion that the concentration of SDS monomers is a crucial factor for SDS–lipase interactions. The presented results are important for the understanding and improvement of protein stability in surfactant systems.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1016/j.abb.2010.11.012

DO - 10.1016/j.abb.2010.11.012

M3 - Journal article

C2 - 21093408

VL - 506

SP - 92

EP - 98

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -

ID: 32374633