Study of the deactivation of Beta-galactosidase entrapped in alginate-carrageenan gels

MAMMARELLA, ENRIQUE; RUBIOLO, AMELIA

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC

Elsevier B.V.

Lugar: BL Delft, The Netherlands; Año: 2005 vol. 34 p. 7 - 13

1381-1177

The effectiveness of Ca-alginate–K-k-carrageenan gels for maintenance stability of matrices formed by the b-galactosidase entrapment during operation conditions were studied by determining the biocatalyst activity behaviour in a batch reactor. The immobilised enzyme thermal deactivation and the biocatalyst protein loss due to gel swelling were investigated after including a mass balance in the enzymatic reaction rate expression. Time-temperature effect was the most important factor in the biocatalyst deactivation reaction. However, results show that the quantity of enzyme entrapped in gels is reduced as it is part of the protein loss. The principal reason of the reduction of enzyme quantity in the biocatalyst was the gel swelling, which was non-linear in the working time and depended on mixing conditions in the reactor. Values were extended for a fixed-bed reactor at similar flow conditions to reduce the error in predicting the results in order to know reactor operation conditions to maintain a constant conversion value. For the reaction conditions analysed, the b-galactosidase entrapment in alginate-carrageenan matrices show good efficiency as immobilisation method.