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Aqueous two-phase systems based on cholinium salts and tetrahydrofuran and their use for lipase purification

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Resumo:Aqueous two-phase systems (ATPS) formed with cholinium-based ionic liquid - ILs (or salts) are a novel, low cost, and high efficient technique for the recovery of biomolecules. This study examines the formation of ATPS based on cholinium-based salts (cholinium chloride, cholinium bitartrate and cholinium dihydrogencitrate) and tetrahydrofuran (THF) for the purification of lipase from Bacillus sp. ITP-001, produced by submerged fermentation. The optimum conditions for this purification were determined to be 40 wt% of THF and 30 wt% of cholinium bitartrate at 25 degrees C. A purification factor of 130.1 +/- 11.7 fold, a lipase yield of 90.0 +/- 0.7% and a partition coefficient of enzyme for IL-rich phase (K-E = 0.11 +/- 0.01) and protein contaminants for THF-rich phase (K-P = 1.16 +/- 0.1) were achieved. (C) 2015 Elsevier B.V. All rights reserved.
Autores principais:Souza, Ranyere L.
Outros Autores:Lima, Rafaella A.; Coutinho, Joao A. P.; Soares, Cleide M. F.; Lima, Alvaro S.
Assunto:IONIC LIQUIDS BIPHASIC SYSTEMS POLYETHYLENE-GLYCOL PROTEIN SEPARATION ASPERGILLUS-NIGER MICROBIAL LIPASES EXTRACTION ECOTOXICITY BIODEGRADATION ACETONITRILE
Ano:2015
País:Portugal
Tipo de documento:artigo
Tipo de acesso:acesso restrito
Instituição associada:Universidade de Aveiro
Idioma:inglês
Origem:RIA - Repositório Institucional da Universidade de Aveiro
Descrição
Resumo:Aqueous two-phase systems (ATPS) formed with cholinium-based ionic liquid - ILs (or salts) are a novel, low cost, and high efficient technique for the recovery of biomolecules. This study examines the formation of ATPS based on cholinium-based salts (cholinium chloride, cholinium bitartrate and cholinium dihydrogencitrate) and tetrahydrofuran (THF) for the purification of lipase from Bacillus sp. ITP-001, produced by submerged fermentation. The optimum conditions for this purification were determined to be 40 wt% of THF and 30 wt% of cholinium bitartrate at 25 degrees C. A purification factor of 130.1 +/- 11.7 fold, a lipase yield of 90.0 +/- 0.7% and a partition coefficient of enzyme for IL-rich phase (K-E = 0.11 +/- 0.01) and protein contaminants for THF-rich phase (K-P = 1.16 +/- 0.1) were achieved. (C) 2015 Elsevier B.V. All rights reserved.