Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571

The objective of this study was to investigate the process of immobilization of inulinases using natural montmorillonite as inorganic support. The enzyme to buffer ratio of 3:10 and 10 min of immobilization led to the highest specific activity, 375.07 U/mg protein. The immobilized inulinase kept its...

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Detalles Bibliográficos
Autores: Coghetto, Chaline C., Scherer, Robison P., Silva, Marceli F., Golunski, Simone, Pergher, Sibele Berenice Castellã, Oliveira, Débora de, Oliveira, J. Vladimir, Treichel, Helen
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2012
País:Brasil
Institución:Universidade Federal do Rio Grande do Norte (UFRN)
Repositorio:Repositório Institucional da UFRN
Idioma:inglés
OAI Identifier:oai:repositorio.ufrn.br:123456789/29187
Acceso en línea:https://repositorio.ufrn.br/jspui/handle/123456789/29187
Access Level:acceso abierto
Palabra clave:Kluyveromyces marxianus NRRL Y-7571
Inulinase
Inorganic support
Immobilization
Descripción
Sumario:The objective of this study was to investigate the process of immobilization of inulinases using natural montmorillonite as inorganic support. The enzyme to buffer ratio of 3:10 and 10 min of immobilization led to the highest specific activity, 375.07 U/mg protein. The immobilized inulinase kept its activity after 1968 h under storage at low temperatures and after 456–1826 h at high temperatures. The pH value of 3.5 led to the highest specific activity. Km values of 1.46 and 0.38 mM, and vmax of 0.2487 and 0.2396 mol/L min, were obtained, respectively, for sucrose and inulin.