Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis
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Data
2012-03
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Resumo
The immobilization of Aspergillus oryzae β-galactosidase was achieved by entrapment in sodium
alginate and gelatin and cross-linking with glutaraldehyde. The optimal concentrations of the aforementioned
variables in the immobilization process were determined using an orthogonal central composite design with an
orthogonal axial value of 1.35313. The concentrations of alginate, gelatin and glutaraldehyde that provided the
greatest enzymatic activity were 6.60%, 4.05% and 3.64% (w/v), respectively. The stability of the immobilized
enzyme under the optimal conditions was evaluated through daily activity assays. After 25 uses, a 20% decrease
in the enzymatic activity was observed, indicating that the immobilization process could be used to produce a
stable biocatalyst. This study investigates the influence of lactose and product concentrations on kinetic reaction
hydrolysis. The concentration ranges for the studied variables were 10 to 56 g/L for lactose and 0 to 11.5 g/L for
glucose and galactose. Only galactose presented a competitive inhibitory effect.
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Alginate, Aspergillus oryzae, β-galactosidase enzyme, Entrapment, Optimization, Gelatin
Citação
FREITAS, F. F. et al. Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis. Brazilian Journal of Chemical Engineering, São Paulo, v. 29, n. 1, p. 15-24, Jan./Mar. 2012.