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Immobilization of beta-glucosidase from Penicillium funiculosum on nylon powder.

Biotechnology and applied biochemistry (1993-02-01)
J Aguado, M D Romero, L Rodríguez
ABSTRACT

beta-Glucosidase from Penicillium funiculosum was immobilized on nylon powder previously activated with triethyloxonium tetrafluoroborate, 1,2-diaminoethane and glutaraldehyde. The activation of the nylon powder and the immobilization processes were studied and optimized for the enzyme and the matrix. A high activity retention (67%) was obtained using the activation and immobilization conditions finally selected.

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Sigma-Aldrich
Triethyloxonium tetrafluoroborate solution, 1.0 M in methylene chloride
Sigma-Aldrich
Triethyloxonium tetrafluoroborate, ≥97.0% (T)