INIQUI   05448
INSTITUTO DE INVESTIGACIONES PARA LA INDUSTRIA QUIMICA
Unidad Ejecutora - UE
artículos
Título:
Immobilization of glucosyltransferase from Erwinia sp. using two different techniques
Autor/es:
FABIANO JARES CONTESINI; CAROLINA IBARGUREN; CARLOS RAIMUNDO FERREIRA GROSSO; PATRÍCIA DE OLIVEIRA CARVALHO; HÉLIA HARUMI SATO
Revista:
JOURNAL OF BIOTECHNOLOGY
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Año: 2012 vol. 158 p. 137 - 143
ISSN:
0168-1656
Resumen:
Two different techniques of glucosyltransferase immobilization were studied for the conversion of sucrose into isomaltulose. The optimum conditions for immobilization of Erwinia sp. glucosyltransferase onto Celite 545, determined using response surface methodology, was pH 4.0 and 170 U of glucosyltransferase/g of Celite 545. Using this conditions more than 60% conversion of sucrose into isomaltulose can be obtained. The immobilization of glucosyltransferase was also studied by its entrapment in microcapsules of low-methoxyl pectin and fat (butter and oleic acid). The non-lyophilized microcapsules of pectin, containing the enzyme and fat, showed higher glucosyltransferase activity, compared with lyophilized microcapsules containing enzyme plus fat, and also lyophilized microcapsules containing enzyme without fat addition. The non-lyophilized microcapsules of pectin containing the glucosyltransferase and fat, converted 30% of sucrose into isomaltulose in the first batch. However the conversion decreased to 5% at the 10th batch, indicating inactivation of the enzyme.