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PublicationPROCESS BIOCHEMISTRY
Year2016
Volume51
Pages875-880
International

ION EXCHANGE Of β-GALACTOSIDASE. THE EFFECT OF THE IMMOBILIZATION pH ON ENZYME STABILITY.

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimización de biocatalizadores y bioprocesos enzimáticos
Tiago L. de Albuquerquea,b,+, Sara Peircea,c, +, Nazzoly Rueda d, Antonio Marzocchellac,
Luciana R.B. Gonçalvesb, Maria Valderez Ponte Rochab, Roberto Fernandez-Lafuentea*
a Departamento de Biocatálisis. Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid. Spain.
b Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455-760, Fortaleza, CE, Brazil.
c Dipartimento di Ingegneria Chimica, dei Materiali e della Produzione Industriale. Universita' degli Studi di Napoli Federico II
d Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia
 
β-galactosidase from Aspergillus oryze has been immobilized at pH 5, 7 and 9 on an aminated support using 5 mM buffer. The immobilization was total in 30 minutes, maintaining 75-80% of activity. These preparations were inactivated at different pH values and in the presence of 50% ethanol. The stability of the enzyme immobilized at pH 9 was much lower than that of the enzyme immobilized at pH 5 under all studied conditions but the differences decreased as the ionic strength of the inactivation solution increased. The likeliest explanation to these different stabilities depending on the immobilization pH was that the enzyme presented a different orientation on the support. The enzyme immobilized at pH 5 was more stable than the free enzyme at pHs 5 and 9 (by a 2 or a 6 fold factor respectively), while  at pH 7 the free enzyme was clearly more stable than the immobilized enzyme. 
Keywords:ionic exchange, enzyme stability, enzyme-support orientation, β-galactosidase, biocatalyst design.
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