Purification of alpha-galactosidase from seeds of Sesbania marginata

AUTOR(ES)

Falco, A.L.P., Durrant, L.R., Franco, T.T.

FONTE

Brazilian Journal of Chemical Engineering

DATA DE PUBLICAÇÃO

2000-12

RESUMO

Alpha-galactosidase taken from a raw extract of Sesbania marginata legume seeds was purified by partitioning in aqueous two-phase systems (ATPS). Initially, galactomannan/dextran 2,000,000 systems were used for the purification, and the partition coefficients of alpha -galactosidase varied from 1.5 to 4.0. However, mass transport in these systems was poor due to the high viscosity of the employed polymers. Therefore, partitioning in polyethyleneglycol (PEG)/ sodium phosphate systems and the effect of sodium chloride upon the enzyme purification and the yield of alpha -galactosidase were also investigated. The purification achieved in a single-step was 5.7 with a recovery of 144% of alpha -galactosidase, possibly due to the removal of materials which inhibited alpha -galactosidase activity before the purification. The removal of the main protein contaminants and the highest yields were achieved in PEG 4,000/ sodium phosphate + 6% NaCl system at pH 5.0. Further purification by preparative on-exchange chromatography was also developed.

Documentos Relacionados

• Purification and characterization of an alpha-galactosidase from Aspergillus fumigatus
• Purification and characterization of thermostable beta-mannanase and alpha-galactosidase from Bacillus stearothermophilus.
• Nucleotide sequence of the human alpha-galactosidase A gene.
• Secretion of the alpha-galactosidase from Cyamopsis tetragonoloba (guar) by Bacillus subtilis.
• Sequence variations in the first exon of alpha-galactosidase A.