Abstract
Native water-soluble enzymes were transformed into interface-binding enzymes via conjugation with hydrophobic polymers, thus enabling interesting interfacial biocatalysis between immiscible chemicals at oil/water interfaces. Such interfacial biocatalysis demonstrated a significantly improved catalytic efficiency as compared to traditional biphasic reactions with enzymes contained in the bulk aqueous phase. Particularly, polystyrene-conjugated β-galactosidase showed a catalytic efficiency that was more than 145 times higher than that of the native enzyme for a transgalactosylation reaction. It is believed that the improved accessibility of the biocatalysts to chemicals held in both phases across the interface is the key driver for the enhancement of enzyme activity.
Original language | English (US) |
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Pages (from-to) | 11132-11133 |
Number of pages | 2 |
Journal | Journal of the American Chemical Society |
Volume | 126 |
Issue number | 36 |
DOIs | |
State | Published - Sep 15 2004 |