Enhanced Heat Stability of α‐Chymotrypsin through Single‐Enzyme Confinement in Attoliter Liposomes |
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| Authors: | Assoc.‐Prof. Dr. Makoto Yoshimoto Jun Yamada Misaki Baba Prof. Dr. Peter Walde |
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| Affiliation: | 1. Department of Applied Molecular Bioscience, Yamaguchi University, Ube, Japan;2. Department of Materials, ETH Zürich, Zürich, Switzerland |
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| Abstract: | The entrapment of α‐chymotrypsin (α‐CT) within 70–140 nm liposomes formed from POPC (1‐palmitoyl‐2‐oleoyl‐sn‐glycero‐3‐phosphocholine) leads to an unexpected and remarkable increase in the thermal stability of the enzyme. This finding is based on the observation that heating aqueous suspensions of α‐CT‐containing POPC liposomes to 80 °C for 30 minutes resulted in partial enzyme inactivation, whereas the same treatment of aqueous solutions of free α‐CT inactivated the enzyme completely. The stabilizing effect of enzyme confinement in the attoliter volumes of the liposomes was found to increase with decreasing numbers of α‐CT molecules per liposome. Single‐enzyme confinement was particularly effective, as intermolecular interactions between heat‐denatured α‐CT molecules (causing irreversible inactivation) are not possible. |
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| Keywords: | chymotrypsin compartment enzymes liposomes stability vesicles |
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