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Merck
CN

Enzyme molecules as nanomotors.

Journal of the American Chemical Society (2013-01-12)
Samudra Sengupta, Krishna K Dey, Hari S Muddana, Tristan Tabouillot, Michael E Ibele, Peter J Butler, Ayusman Sen
ABSTRACT

Using fluorescence correlation spectroscopy, we show that the diffusive movements of catalase enzyme molecules increase in the presence of the substrate, hydrogen peroxide, in a concentration-dependent manner. Employing a microfluidic device to generate a substrate concentration gradient, we show that both catalase and urease enzyme molecules spread toward areas of higher substrate concentration, a form of chemotaxis at the molecular scale. Using glucose oxidase and glucose to generate a hydrogen peroxide gradient, we induce the migration of catalase toward glucose oxidase, thereby showing that chemically interconnected enzymes can be drawn together.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Glucose Oxidase from Aspergillus niger, Type VII, lyophilized powder, ≥100,000 units/g solid (without added oxygen)
Sigma-Aldrich
Glucose Oxidase from Aspergillus niger, Type X-S, lyophilized powder, 100,000-250,000 units/g solid (without added oxygen)
Sigma-Aldrich
Urease from Canavalia ensiformis (Jack bean)
Sigma-Aldrich
Urease from Canavalia ensiformis (Jack bean), Type III, glycerol solution, 500-800 units/mL
Sigma-Aldrich
Urease from Canavalia ensiformis (Jack bean), Type C-3, powder, ≥600,000 units/g solid
Sigma-Aldrich
Urease from Canavalia ensiformis (Jack bean), Type III, powder, 15,000-50,000 units/g solid
Sigma-Aldrich
Urease from Canavalia ensiformis (Jack bean), Type IX, powder, 50,000-100,000 units/g solid
Sigma-Aldrich
Urease from Canavalia ensiformis (Jack bean), powder, white, ~8 U/mg
Sigma-Aldrich
Urease from Canavalia ensiformis (Jack bean), powder, ~1 U/mg