Hydrostatic Pressure Increases the Catalytic Activity of Amyloid Fibril Enzymes. Issue 40 (30th August 2016)

• Record Type: Journal Article
• Authors: Luong, Trung Quan; Erwin, Nelli; Neumann, Matthias; Schmidt, Andreas; Loos, Cornelia; Schmidt, Volker; Fändrich, Marcus; Winter, Roland
• Is Part Of: Angewandte Chemie international edition. Volume 55:Issue 40(2016)
• Page Start: 12412
• Page End: 12416
• Publication Date: 2016-08-30
• Subjects: amyloid fibrils -- catalysis -- pressure -- stopped-flow techniques; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201605715
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: We studied the combined effects of pressure (0.1–200 MPa) and temperature (22, 30, and 38 °C) on the catalytic activity of designed amyloid fibrils using a high‐pressure stopped‐flow system with rapid UV/Vis absorption detection. Complementary FT‐IR spectroscopic data revealed a remarkably high pressure and temperature stability of the fibrillar systems. High pressure enhances the esterase activity as a consequence of a negative activation volume at all temperatures (about −14 cm 3 mol −1 ). The enhancement is sustained in the whole temperature range covered, which allows a further acceleration of the enzymatic activity at high temperatures (activation energy 45–60 kJ mol −1 ). Our data reveal the great potential of using both pressure and temperature modulation to optimize the enzyme efficiency of catalytic amyloid fibrils. Abstract : Negative+positive=better catalysis : Studying the combined effects of pressure and temperature on the hydrolysis of p ‐nitrophenyl acetate catalyzed by designed amyloid fibrils using high‐pressure stopped‐flow techniques with rapid UV/Vis absorbance detection showed that both pressure and temperature effectively enhance the catalysis as a consequence of a negative activation volume and a positive activation energy.