Polymer-enzyme conjugates can self-assemble at oil/water interfaces and effect interfacial biotransformations.
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 beta-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.
Zhu
Guangyu
G
Department of Chemical Engineering, The University of Akron, Akron, Ohio 44325-3906, USA.
Wang
Ping
P
D002918:Chymotrypsin / Q000737:chemistry* / Q000378:metabolism; D004795:Enzyme Stability; D007700:Kinetics; D007785:Lactose / Q000737:chemistry / Q000378:metabolism; D011137:Polystyrenes / Q000737:chemistry*; D013499:Surface Properties; D014050:Toluene / Q000737:chemistry; D014867:Water / Q000737:chemistry; D001616:beta-Galactosidase / Q000737:chemistry* / Q000378:metabolism
D011137:Polystyrenes; D014867:Water; D014050:Toluene; D001616:beta-Galactosidase; D002918:Chymotrypsin; C117608:alpha-chymotrypsin; D007785:Lactose