CAMPERI Silvia Andrea
Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interes
NANCY B. IANNUCCI; FEDERICO J. WOLMAN; SILVIA A. CAMPERI; AGUSTÍN A. NAVARRO DEL CAÑIZO; MARIANO GRASSELLI; OSVALDO CASCONE
BRAZILIAN JOURNAL OF CHEMICAL ENGINEERING
Año: 2003 vol. 20 p. 27 - 27
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.