Hydrostatic Pressure Increases the Catalytic Activity of Amyloid Fibril Enzymes |
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Authors: | Dr Trung Quan Luong Nelli Erwin Matthias Neumann Andreas Schmidt Cornelia Loos Prof?Dr Volker Schmidt Prof?Dr Marcus Fändrich Prof?Dr Roland Winter |
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Institution: | 1. Fakult?t für Chemie und Chemische Biologie, TU Dortmund, Dortmund, Germany;2. Institut für Stochastik, Universit?t Ulm, Germany;3. Institut für Pharmazeutische Biotechnologie, Universit?t Ulm, Ulm, Germany |
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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 cm3 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. |
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Keywords: | amyloid fibrils catalysis pressure stopped-flow techniques |
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