Immobilization of Aspergillus oryzae Β-galactosidase in an agarose matrix functionalized by four different methods and application to the synthesis of lactulose

Cecilia Guerrero, Carlos Vera, Nestor Serna, Andrés Illanes

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

33 Citas (Scopus)

Resumen

Aspergillus oryzae β-galactosidase was immobilized in monofunctional glyoxyl-agarose and heterofunctional supports (amino-glyoxyl, carboxy-glyoxyl and chelate-glyoxyl agarose), for obtaining highly active and stable catalysts for lactulose synthesis. Specific activities of the amino-glyoxyl agarose, carboxy-glyoxyl agarose and chelate-glyoxyl agarose derivatives were 3676, 430 and 454 IU/g biocatalyst with half-life values at 50 °C of 247, 100 and 100 h respectively. Specific activities of 3490, 2559 and 1060 IU/g were obtained for fine, standard and macro agarose respectively. High immobilization yield (39.4%) and specific activity of 7700 IU/g was obtained with amino-glyoxyl-agarose as support. The highest yields of lactulose synthesis were obtained with monofunctional glyoxyl-agarose. Selectivity of lactulose synthesis was influenced by the support functionalization: glyoxyl-agarose and amino-glyoxyl-agarose derivatives retained the selectivity of the free enzyme, while selectivity with the carboxy-glyoxyl-agarose and chelate-glyoxyl-agarose derivatives was reduced, favoring the synthesis of transgalactosylated oligosaccharides over lactulose.

Idioma originalInglés
Páginas (desde-hasta)53-63
Número de páginas11
PublicaciónBioresource Technology
Volumen232
DOI
EstadoPublicada - 2017
Publicado de forma externa

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