dc.creatorIllanes, Andrés
dc.creatorWilson, Lorena
dc.creatorAguirre Céspedes, Carolina
dc.date2015-11-25T13:47:09Z
dc.date2015-11-25T13:47:09Z
dc.date2009
dc.identifierApplied Biochemistry and Biotechnology 157
dc.identifier1559-0291
dc.identifierhttp://repositoriodigital.ucsc.cl/handle/25022009/520
dc.descriptionArtículo de publicación ISI
dc.descriptionThe use of very high substrate concentrations favors the kinetically controlled synthesis of cephalexin with penicillin acylase (PA) not only by Michaelian considerations, but also because water activity is depressed, so reducing the rates of the competing reactions of product and acyl donor hydrolysis. Commercial PGA-450, glyoxyl agarose immobilized (PAIGA) and carrier-free cross-linked enzyme aggregates of penicillin acylase (PACLEA) were tested in aqueous media at concentrations close to the solubility of nucleophile and at previously determined enzyme to nucleophile and acid donor to nucleophile ratios. The best temperature and pH were determined for each biocatalyst based on an objective function considering conversion yield, productivity, and enzyme stability as evaluation parameters. Stability was higher with PAIGA and specific productivity higher with PACLEA, but best results based on such objective function were obtained with PGA-450. Yields were stoichiometric and productivities higher than those previously reported in organic medium, which implies significant savings in terms of costs and environmental protection. At the optimum conditions for the selected biocatalyst, operational stability was determined in sequential batch reactor operation. The experimental information gathered is being used for a technical and economic evaluation of an industrial process for enzymatic production of cephalexin in aqueous medium
dc.languageen
dc.publisherSpringer
dc.sourcehttp://goo.gl/3eMjwX
dc.subjectPenicillin acylase
dc.subjectEnzyme immobilization
dc.subjectCephalexin
dc.subjectCross-linked enzyme aggregates
dc.subjectMultipoint covalent attachment
dc.titleSynthesis of cephalexin in aqueous medium with carrier-bound and carrier-free penicillin acylase biocatalysts
dc.typeArtículos de revistas


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