Open AccessAffinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest
Author(s) -
Nancy B. Iannucci,
Federico Javier Wolman,
Silvia A. Camperi,
Agustín A. Navarro del Cañizo,
Mariano Grasselli,
Osvaldo Cascone
Publication year - 2003
Publication title -
brazilian journal of chemical engineering/brazilian journal of chemical engineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.313
H-Index - 52
eISSN - 1678-4383
pISSN - 0104-6632
DOI - 10.1590/s0104-66322003000100006
Subject(s) - iminodiacetic acid , chemistry , agarose , chromatography , affinity chromatography , membrane , fractionation , protease , enzyme , specific activity , biochemistry , chelation , organic chemistry
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