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Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
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Activity of soluble and immobilized hesperidinase on insoluble hesperidin
M A Sánchez1, C Romero1, A Manjón1
1Department of Biochemistry and Molecular Biology. Faculty of Chemistry, University of Murcia, 30001, Murcia, Spain.
Biotechnology Letters
|March 2, 2017
Abstract:
A michaelian kinetic behaviour was found when the α-ramnosidase activity, both of native and immobilized hesperidinase, was determined on hesperidin suspensions. In spite of the low hesperidin solubility in the reaction medium, the maximum rates overtook the expected values, thus pointing to the enzyme ability to degrade insoluble hesperidin.

