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Thermomyces lanuginosus lipase in the liquid-crystalline phases of aqueous phytantriol: X-ray diffraction and vibrational spectroscopic studies

Misiunas, A.; Talaikyte, Z.; Niaura, G.; Razumas, V. and Nylander, Tommy LU (2008) In Biophysical Chemistry 134(3). p.144-156
Abstract
The influence of Thermomyces lanuginosus lipase (TLL) on the phase behaviour of liquid-crystalline phases of aqueous phytantriol as well as conformational changes of TLL entrapped in the cubic Q(230) phase have been studied by small angle X-ray diffraction (SAXD), FT-Raman, and FT-IR techniques. It was found that the lipidic Q(230) Phase is able to accommodate up to 10 wt.% of TLL, and the temperature of phase transition to the inverted hexagonal phase H-11 increases indicating stabilizing effect of the protein. FT-Raman analysis of Trp amino acid marker band W3 revealed that the average rotation angle around the C-3 - C-beta bond of four TLL residues of TLL in the Q(230) phase increases. Reasoning from available TLL crystallographic data,... (More)
The influence of Thermomyces lanuginosus lipase (TLL) on the phase behaviour of liquid-crystalline phases of aqueous phytantriol as well as conformational changes of TLL entrapped in the cubic Q(230) phase have been studied by small angle X-ray diffraction (SAXD), FT-Raman, and FT-IR techniques. It was found that the lipidic Q(230) Phase is able to accommodate up to 10 wt.% of TLL, and the temperature of phase transition to the inverted hexagonal phase H-11 increases indicating stabilizing effect of the protein. FT-Raman analysis of Trp amino acid marker band W3 revealed that the average rotation angle around the C-3 - C-beta bond of four TLL residues of TLL in the Q(230) phase increases. Reasoning from available TLL crystallographic data, this result is explained by structural transition of entrapped protein to so-called "open" and more related to the enzymaticallyactive conformation. TLL secondary structure analysis by amide I and amide III vibrational bands showed that content of alpha-helixes does not change, while a part of beta-sheet structures transforms to less ordered elements upon incorporation of protein into the Q230 phase of aqueous phytantriol. (c) 2008 Elsevier B.V. All rights served. (Less)
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subject
keywords
TRYPTOPHAN SIDE-CHAINS, INDUCED, CONFORMATIONAL-CHANGES, SECONDARY STRUCTURE ESTIMATION, RHIZOPUS-ARRHIZUS LIPASE, HUMICOLA-LANUGINOSA, RAMAN-SPECTROSCOPY, FUNGAL LIPASE, CUBIC PHASES, INTERFACIAL ACTIVATION, TRANSFORM INFRARED-SPECTROSCOPY, aqueous liquid-crystalline, spectroscopy, phytantriol, Thermomyces lanuginosus lipase, Raman, FT-IR spectroscopy, phases, small angle X-ray diffraction (SAXD)
in
Biophysical Chemistry
volume
134
issue
3
pages
144 - 156
publisher
Elsevier
external identifiers
  • wos:000255676900003
  • scopus:41449114089
ISSN
1873-4200
DOI
10.1016/j.bpc.2008.02.002
language
English
LU publication?
yes
id
24ec4520-27aa-415c-87ee-5962f53a01d3 (old id 1417370)
date added to LUP
2009-06-12 12:01:19
date last changed
2017-02-26 03:54:39
@article{24ec4520-27aa-415c-87ee-5962f53a01d3,
  abstract     = {The influence of Thermomyces lanuginosus lipase (TLL) on the phase behaviour of liquid-crystalline phases of aqueous phytantriol as well as conformational changes of TLL entrapped in the cubic Q(230) phase have been studied by small angle X-ray diffraction (SAXD), FT-Raman, and FT-IR techniques. It was found that the lipidic Q(230) Phase is able to accommodate up to 10 wt.% of TLL, and the temperature of phase transition to the inverted hexagonal phase H-11 increases indicating stabilizing effect of the protein. FT-Raman analysis of Trp amino acid marker band W3 revealed that the average rotation angle around the C-3 - C-beta bond of four TLL residues of TLL in the Q(230) phase increases. Reasoning from available TLL crystallographic data, this result is explained by structural transition of entrapped protein to so-called "open" and more related to the enzymaticallyactive conformation. TLL secondary structure analysis by amide I and amide III vibrational bands showed that content of alpha-helixes does not change, while a part of beta-sheet structures transforms to less ordered elements upon incorporation of protein into the Q230 phase of aqueous phytantriol. (c) 2008 Elsevier B.V. All rights served.},
  author       = {Misiunas, A. and Talaikyte, Z. and Niaura, G. and Razumas, V. and Nylander, Tommy},
  issn         = {1873-4200},
  keyword      = {TRYPTOPHAN SIDE-CHAINS,INDUCED,CONFORMATIONAL-CHANGES,SECONDARY STRUCTURE ESTIMATION,RHIZOPUS-ARRHIZUS LIPASE,HUMICOLA-LANUGINOSA,RAMAN-SPECTROSCOPY,FUNGAL LIPASE,CUBIC PHASES,INTERFACIAL ACTIVATION,TRANSFORM INFRARED-SPECTROSCOPY,aqueous liquid-crystalline,spectroscopy,phytantriol,Thermomyces lanuginosus lipase,Raman,FT-IR spectroscopy,phases,small angle X-ray diffraction (SAXD)},
  language     = {eng},
  number       = {3},
  pages        = {144--156},
  publisher    = {Elsevier},
  series       = {Biophysical Chemistry},
  title        = {Thermomyces lanuginosus lipase in the liquid-crystalline phases of aqueous phytantriol: X-ray diffraction and vibrational spectroscopic studies},
  url          = {http://dx.doi.org/10.1016/j.bpc.2008.02.002},
  volume       = {134},
  year         = {2008},
}