Abstract

Abstract The adsorption characteristics of commercial amyloglucosidase enzyme preparation from Aspergillus niger on the β-cyclodextrin-chitosan system were studied. The effects of pH, temperature, and ionic strength on the equilibrium partition coefficients were investigated in order to obtain the optimum process conditions for a possible AMG purification scheme. It was shown that the adsorption isotherm for this system at pH 4.5 at ambient temperature obeyed the Langmuir relationship, and the Langmuir parameters of q m and K p were estimated as 120.5 mg/mL hydrated gel and 1.4 mg/mL solvent, respectively. The complete elution of the enzyme from the matrix was achieved with an increase in pH by using 0.1 M borate buffer, pH 8.0.

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