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β-Galactosidase from Aspergillus oryzae has been immobilized at pH 5, 7 and 9 on an aminated support using 5mM buffer. The immobilization was total in 30min, maintaining 75–80% of activity. These preparations were inactivated at different pH values and in the presence of 50% ethanol. The stability of the enzyme immobilized at pH 9 was much lower than that of the enzyme immobilized at pH 5 under all...
In this review, we detail the efforts performed to couple the purification and the immobilization of industrial enzymes in a single step. The use of antibodies, the development of specific domains with affinity for some specific supports will be revised. Moreover, we will discuss the use of domains that increase the affinity for standard matrices (ionic exchangers, silicates). We will show how the...
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