S-layer proteins as a source of carotenoids: Isolation of the carotenoid cofactor deinoxanthin from its S-layer protein DR_2577

FARCI, DOMENICA;ESPOSITO, FRANCESCA;PIANO, DARIO
2017-01-01

Abstract

S-layers are regular paracrystalline arrays of proteins or glycoproteins that characterize the outer envelope of several bacteria and archaea. The auto-assembling properties of these proteins make them suitable for application in nanotechnologies. However, the bacterial cell wall and its S-layer are also an important binding sites for carotenoids and they may represent a potential source of these precious molecules for industrial purposes. The S-layer structure and its components were extensively studied in the radio-resistant bacterium . Deinococcus radiodurans, which for long time represented one of the model organisms in this respect. The protein DR_2577 has been shown to be one of the naturally over-expressed S-layer components in this bacterium. The present report describes a high scale purification procedure of this protein in solution. The purity of the samples, assayed by native and denaturing electrophoresis, showed how this method leads to a selective and high efficient recovery of the pure DR_2577. Recently, we have found that the deinoxanthin, a carotenoid typical of . D. radiodurans, is a cofactor non covalently bound to the protein DR_2577. The pure DR_2577 samples may be precipitated or lyophilized and used as a source of the carotenoid cofactor deinoxanthin by an efficient extraction using organic solvents. The procedure described in this work may represent a general approach for the isolation of S-layer proteins and their carotenoids with potentials for industrial applications.
2017
2016
Inglese
99
pt 2
868
876
9
Esperti anonimi
internazionale
scientifica
Carotenoids; Cold extrusion; Deinococcus radiodurans; Deinoxanthin; DR_2577; French pressure cell; S-layer; Xanthophyll; Food science
Farci, Domenica; Esposito, Francesca; El Alaoui, Sabah; Piano, Dario
1.1 Articolo in rivista
info:eu-repo/semantics/article
1 Contributo su Rivista::1.1 Articolo in rivista
262
4
partially_open
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