Immobilization of lipase from Pseudomonas fluorescens on glyoxyl-octyl-agarose beads: Improved stability and reusability

Authors: Rios, NS; Mendez-Sanchez, C; Arana-Pena, S; Rueda, N; Ortiz, C; Goncalves, LRB; Fernandez-Lafuente, R

Article.
BBA-Proteins Proteomics. vol: 1867. page: 1570-9639.
Date: SEP. 2019.
Doi: 10.1016/j.bbapap.2019.06.005.

Abstract:
The lipase from Pseudomonas fluorescens (PFL) has been immobilized on glyoxyl-octyl agarose and compared to the enzyme immobilized on octyl-agarose. Thus, PFL was immobilized at pH 7 on glyoxyl-octyl support via lipase interfacial activation [read more]

A new mechanistic model for an O-2-protected electron-bifurcating hydrogenase, Hnd from Desulfovibrio fructosovorans

Authors: Kpebe, A; Benvenuti, M; Guendon, C; Rebai, A; Fernandez, V; Le Laz, S; Etienne, E; Guigliarelli, B; Garcia-Molina, G; de Lacey, AL; Baffert, C; Brugna, M

Article.
Biochim. Biophys. Acta-Bioenerg.. vol: 1859. page: 0005-2728.
Date: DEC. 2018.
Doi: 10.1016/j.bbabio.2018.09.364.

Abstract:
The genome of the sulfate-reducing and anaerobic bacterium Desulfovibrio fructosovorans encodes different hydrogenases. Among them is Hnd, a tetrameric cytoplasmic [FeFe] [read more]

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Biochemistry & Molecular Biology; Biophysics

Immobilization of lipase from Pseudomonas fluorescens on glyoxyl-octyl-agarose beads: Improved stability and reusability

A new mechanistic model for an O-2-protected electron-bifurcating hydrogenase, Hnd from Desulfovibrio fructosovorans

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