Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest

AUTOR(ES)

Iannucci, N.B., Wolman, F.J., Camperi, S.A., Cañizo, A.A.N., Grasselli, M., Cascone, O.

FONTE

Brazilian Journal of Chemical Engineering

DATA DE PUBLICAÇÃO

2003-03

RESUMO

High-performance affinity matrices were obtained by attaching pseudobiospecific ligands to hollow-fibre membranes. The neutral protease contained in FlavourzymeTM was purified to homogeneity with Yellow 4R-HE affinity hollow-fibre membranes. Immobilisation of Red HE-3B allowed purification of a milk-clotting enzyme obtained by solid-state culture of Mucor bacilliformis. Copper immobilisation through iminodiacetic acid allowed fractionation of Biocon Bioconcentrated PlusTM to separate the pectinesterase-containing fraction. The productivity of the developed processes - 1900, 94 and 750 U/ml.min, respectively - was 10- to 15-fold higher than that achieved with the same ligands immobilised on agarose-based soft gels, mainly due to the shortening of the purification processes.

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