摘要：SummaryThe stability of protein structures and biological functions at normal temperature is closely linked with the universal aqueous environment of organisms. Preserving bioactivities of proteins in hyperthermia water would expand their functional capabilities beyond those in native environments. However, only a limited number of proteins derived from hyperthermophiles are thermostable at elevated temperatures. Triggered by this, here we describe a general method to stabilize mesophilic proteins in hyperthermia water. The mesophilic proteins, protected by amphiphilic polymers with multiple binding sites, maintain their secondary and tertiary structures after incubation even in boiling water. This approach, outside the conventional environment for bioactivities of mesophilic proteins, provides a general strategy to dramatically increase the Tm(melting temperature) of mesophilic proteins without any changes to amino sequences of the native proteins. Current work offers a new insight with protein stability engineering for potential application, including vaccine storage and enzyme engineering.Graphical abstractDisplay OmittedHighlights•Preserving bioactivities of proteins in hyperthermia water is promising.•Amphiphilic polymers could protect mesophilic proteins even in boiling water.•Mesophilic proteins protected by amphiphilic polymers show dramatically increased Tm.•The method offers application prospect for vaccine storage and enzyme engineering.Polymer chemistry ; Protein ; Bioengineering ; Biomaterials.
