Purification and biochemical characterization of photo-active membrane protein bacteriorhodopsin from Haloarcula marismortui, an extreme halophile from the Dead Sea.
Int J Biol Macromol
; 118(Pt B): 1942-1947, 2018 Oct 15.
Article
en En
| MEDLINE
| ID: mdl-30017983
ABSTRACT
Bacteriorhodopsin (BR) is an exciting photo-active retinal protein with many potential industrial applications. In this study, BR from the extremely halophilic archaeon Haloarcula marismortui (HmBR) was purified successfully using aqueous two phase extraction method. Absorption spectroscopy analysis showed maximum absorption peak of HmBR retinal protein (λmax) at 415â¯nm. The purified HmBR was visualized by SDS-PAGE, with a subunit molecular mass of 27â¯kDa, and its identity was confirmed by resonance Raman spectroscopy, Fourier transform infrared spectroscopy and atomic force microscopy. The effect of pH and salt concentration on the absorption spectrum of HmBR was evaluated. Red-shifted in λmax of HmBR was recorded at acidic condition (pHâ¯5) and HmBR showed remarkable optical activity under high salinity condition. The photoelectric activity of HmBR was evaluated by measuring the DC-voltage generated from HmBR coated on indium tin oxide (ITO) glass when light illumination was applied.
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Banco de datos:
MEDLINE
Asunto principal:
Bacteriorodopsinas
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Haloarcula marismortui
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Luz
Idioma:
En
Año:
2018
Tipo del documento:
Article