Abstract
Abstract A lipid-coated β-D-galactosidase could act as an efficient catalyst for transgalactosylation in the water-organic two phases: both the hydrophobic lipid-coated enzyme and alcohols were solubilized in isopropyl ether and mixed with an aqueous solution of lactose (a galactosyl donor). When a native β-D-galactosidase was employed for the same reaction, neither the transgalactosylation nor the hydrolysis reaction proceeded due to the deactivation of the enzyme at the interface.
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