Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/80737
Type: Artigo de periódico
Title: Recovery of aprotinin from insulin industrial process effluent by affinity adsorption
Author: Azzoni, AR
Miranda, EA
Abstract: Aprotinin is a protease inhibitor found in bovine organs and used as a valuable human therapeutic compound. In this work, a process for the recovery of aprotinin from insulin industrial process effluent via affinity adsorption on immobilized trypsin and chymotrypsin was developed. First, process conditions were set as a result of a study of the effects of pH and ionic strength on pure aprotinin adsorption and desorption utilizing an experimental design methodology. The best conditions obtained with immobilized trypsin as the ligand were adsorption at 0.018 M NaCl and pH 8.7 and desorption at 0.018 M NaCl and pH 2.1. For immobilized chymotrypsin, the best conditions were adsorption at 0.582 M NaCl and pH 8.0 and desorption at 0.582 M NaCl and pH 2.1. Recovery of the inhibitor from the effluent was carried out utilizing a two-step process: trypsin agarose adsorption followed by chymotrypsin-agarose adsorption. Analysis of the chromatographic fractions by trypsin and chymotrypsin inhibition and capillary electrophoresis assays strongly suggested that the recovered inhibitor is aprotinin.
Country: EUA
Editor: Springer Verlag
Rights: fechado
Identifier DOI: 10.1007/s004490050716
Date Issue: 1999
Appears in Collections:Unicamp - Artigos e Outros Documentos

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