Recovery and purification of aprotinin from industrial insulin-processing effluent by immobilized chymotrypsin and negative IMAC chromatographies

dc.creatorde Genaro, ACB
dc.creatorTamagawa, RE
dc.creatorAzzoni, AR
dc.creatorBueno, SMA
dc.creatorMiranda, EA
dc.date2002
dc.dateJUL
dc.date2014-11-17T23:58:47Z
dc.date2015-11-26T16:47:57Z
dc.date2014-11-17T23:58:47Z
dc.date2015-11-26T16:47:57Z
dc.date.accessioned2018-03-28T23:34:16Z
dc.date.available2018-03-28T23:34:16Z
dc.identifierProcess Biochemistry. Elsevier Sci Ltd, v. 37, n. 12, n. 1413, n. 1420, 2002.
dc.identifier1359-5113
dc.identifierWOS:000176219300010
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/80735
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/80735
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/80735
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1274985
dc.descriptionAprotinin, a bovine protease inhibitor currently also produced in recombinant bacteria, yeast, and corn, has valuable applications as a human therapeutic and in tissue culture. The objective of this work was to develop the basis of a large-scale aprotinin purification process centered on immobilized metal ion affinity chromatography (IMAC). This technique uses ligands-metal ions-of a lower cost and higher stability than those traditionally used in affinity chromatography. Since aprotinin does not interact with IMAC ligands, collection is from the nonretained fractions (negative chromatography). Stirred-tank batch IMAC adsorption experiments indicated that one-step aprotinin purification could not be successful. Immobilized chymotrypsin chromatography was then used as a prepurification step, yielding a suitable feed for IMAC (with purification factors as high as 476). IMAC column fed with these prepurified materials produced purified aprotinin in the nonretained fractions with purification factors as high as 952. (C) 2002 Elsevier Science Ltd. All rights reserved.
dc.description37
dc.description12
dc.description1413
dc.description1420
dc.languageen
dc.publisherElsevier Sci Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationProcess Biochemistry
dc.relationProcess Biochem.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectIMAC
dc.subjectpurification
dc.subjectaprotinin
dc.subjectnegative chromatography
dc.subjectaffinity
dc.subjectProtein
dc.subjectAdsorption
dc.titleRecovery and purification of aprotinin from industrial insulin-processing effluent by immobilized chymotrypsin and negative IMAC chromatographies
dc.typeArtículos de revistas


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