Artigo Revisado por pares

Direct lysozyme separation from egg white by dye membrane affinity chromatography

1999; Wiley; Volume: 79; Issue: 2 Linguagem: Inglês

10.1002/(sici)1097-0010(199902)79

ISSN

1097-0010

Autores

Mariano Grasselli, Silvia A. Camperi, Agustin A Navarro del Ca�izo, Osvaldo Cascone,

Tópico(s)

Advanced Drug Delivery Systems

Resumo

Journal of the Science of Food and AgricultureVolume 79, Issue 2 p. 333-339 Paper Direct lysozyme separation from egg white by dye membrane affinity chromatography Mariano Grasselli, Mariano Grasselli Cátedra de Microbiología Industrial y Biotecnología, Facultad de Farmacia y Bioquímica (UBA), Junín 956, (1113) Buenos Aires, ArgentinaSearch for more papers by this authorSilvia A Camperi, Silvia A Camperi Cátedra de Microbiología Industrial y Biotecnología, Facultad de Farmacia y Bioquímica (UBA), Junín 956, (1113) Buenos Aires, ArgentinaSearch for more papers by this authorAgustin A Navarro del Cañizo, Agustin A Navarro del Cañizo Cátedra de Microbiología Industrial y Biotecnología, Facultad de Farmacia y Bioquímica (UBA), Junín 956, (1113) Buenos Aires, ArgentinaSearch for more papers by this authorOsvaldo Cascone, Corresponding Author Osvaldo Cascone Cátedra de Microbiología Industrial y Biotecnología, Facultad de Farmacia y Bioquímica (UBA), Junín 956, (1113) Buenos Aires, ArgentinaCampichuelo 103–2°A,(1405) Buenos Aires, ArgentinaSearch for more papers by this author Mariano Grasselli, Mariano Grasselli Cátedra de Microbiología Industrial y Biotecnología, Facultad de Farmacia y Bioquímica (UBA), Junín 956, (1113) Buenos Aires, ArgentinaSearch for more papers by this authorSilvia A Camperi, Silvia A Camperi Cátedra de Microbiología Industrial y Biotecnología, Facultad de Farmacia y Bioquímica (UBA), Junín 956, (1113) Buenos Aires, ArgentinaSearch for more papers by this authorAgustin A Navarro del Cañizo, Agustin A Navarro del Cañizo Cátedra de Microbiología Industrial y Biotecnología, Facultad de Farmacia y Bioquímica (UBA), Junín 956, (1113) Buenos Aires, ArgentinaSearch for more papers by this authorOsvaldo Cascone, Corresponding Author Osvaldo Cascone Cátedra de Microbiología Industrial y Biotecnología, Facultad de Farmacia y Bioquímica (UBA), Junín 956, (1113) Buenos Aires, ArgentinaCampichuelo 103–2°A,(1405) Buenos Aires, ArgentinaSearch for more papers by this author First published: 04 May 1999 https://doi.org/10.1002/(SICI)1097-0010(199902)79:2 3.0.CO;2-LCitations: 17AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract An affinity membrane from hydrophylised polyethylene hollow fibre as the support matrix was prepared. Red HE-3B was immobilised on the membrane and the adsorption behaviour of pure lysozyme solutions and homogenised egg white was investigated. Dye density (1.7 μmol ml−1) and maximum binding capacity (26 mg lysozyme ml−1) are comparable to those of commercial gel matrices. Dynamic binding capacity did not change when residence time was reduced from 3 to 1 min. A method for direct lysozyme separation from egg white was developed, with a productivity of 12 kg lysozyme m−3 h−1. The purity of the eluted lysozyme, as determined by HPLC, was 88%, with a recovery of 92%. Dynamic capacity was kept constant at 70% of the maximum binding capacity for at least 10 cycles through membrane regeneration with 0.1 M NaOH and 1 M NaCl. Functional properties of egg white, as judged by viscosity and foaming capacity measurements, did not change after the chromatographic lysozyme depletion. © 1999 Society of Chemical Industry Citing Literature Volume79, Issue2February 1999Pages 333-339 RelatedInformation

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