Effect of sodium dodecylbenzene sulfonate on subtilisin Carlsberg proteolysis of an immobilized ovalbumin film.
Enzymatic degradation of immobilized ovalbumin multilayer films by subtilisin Carlsberg was investigated using in situ ellipsometry. Changes in the substrate cleavage rate in the presence of an anionic surfactant, sodium dodecylbenzene sulfonate (SDBS), were assessed. Exposure of the protein film to SDBS prior to introduction of the enzyme increased the measured proteolysis rate threefold. Surfactant increased the measured film thickness, absorbing into the protein film and causing swelling. Surfactant-induced film swelling was reversible upon aqueous rinsing. Nevertheless, exposure of enzyme to the surfactant-rinsed film increased the proteolysis rate, most likely due to irreversible conformational changes induced in the substrate film by the surfactant. Simultaneous addition of SDBS with enzyme after the initial surfactant exposure did not produce additional protein-removal benefit.
Foose
Ladan L
LL
Department of Chemical Engineering, University of California, Berkeley, California 94720, USA.
Blanch
Harvey W
HW
Radke
C J
CJ
D001557:Benzenesulfonates / Q000494:pharmacology*; D020536:Enzyme Activators / Q000494:pharmacology*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D010047:Ovalbumin; D013381:Subtilisins / Q000378:metabolism*
D001557:Benzenesulfonates; D020536:Enzyme Activators; D004800:Enzymes, Immobilized; C001114:dodecylbenzenesulfonic acid; D010047:Ovalbumin; D013381:Subtilisins