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Continuous production of ß-cyclodextrin from starch by highly stable cyclodextrin glycosyltransferase immobilized on chitosan.
Schöffer, Jéssie da Natividade; Klein, Manuela Poletto; Rodrigues, Rafael C; Hertz, Plinho Francisco.
Afiliación
  • Schöffer Jda N; Biotechnology, Bioprocess and Biocatalysis Group, Institute of Food Science and Technology, Federal University of Rio Grande do Sul, Avenida Bento Gonçalves, 9500, P.O. Box 15090, ZC 91501-970, Porto Alegre, RS, Brazil.
Carbohydr Polym ; 98(2): 1311-6, 2013 Nov 06.
Article en En | MEDLINE | ID: mdl-24053808
Cyclodextrin glycosyltransferase (CGTase) from Thermoanaerobacter sp. was covalently immobilized on glutaraldehyde-activated chitosan spheres and used in a packed bed reactor to investigate the continuous production of ß-cyclodextrin (ß-CD). The optimum temperatures were 75 °C and 85 °C at pH 6.0, respectively for free and immobilized CGTase, and the optimum pH (5.0) was the same for both at 60 °C. In the reactor, the effects of flow rate and substrate concentration in the ß-CD production were evaluated. The optimum substrate concentration was 4% (w/v), maximizing the ß-CD production (1.32 g/L) in a flow rate of 3 mL/min. In addition, the biocatalyst had good operational stability at 60 °C, maintaining 61% of its initial activity after 100 cycles of batch and 100% after 100 h of continuous use. These results suggest the possibility of using this immobilized biocatalyst in continuous production of CDs.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Almidón / Proteínas Bacterianas / Beta-Ciclodextrinas / Enzimas Inmovilizadas / Glucosiltransferasas Idioma: En Revista: Carbohydr Polym Año: 2013 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Almidón / Proteínas Bacterianas / Beta-Ciclodextrinas / Enzimas Inmovilizadas / Glucosiltransferasas Idioma: En Revista: Carbohydr Polym Año: 2013 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Reino Unido