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• W2901364088 abstract "Self-assembling amphipathic peptides (SAPs) have been used as stabilization tags to improve enzyme stability but do not function uniformly well with all target enzymes. Here, the key factors involved in SAPs stabilization were identified as the SAP length and linker length and flexibility, using S1 (AEAEAKAK)2 as an originated SAP and polygalacturonate lyase (PGL) as model protein. Biochemical analysis demonstrated that SAPs could induce loose protein oligomerization via intermolecular hydrophobic interactions. Based on this mechanism, a comprehensive protein stabilization strategy was proposed, in which a library of stabilizing tags through random combination of different SAPs and linker peptides was developed to design the fusion composition while the sodium chloride (NaCl) was used to enhance the intermolecular hydrophobic interactions. By using the strategy, the PGL, lipoxygenase (LOX) and L-asparaginase exhibited 33.25-, 17.55- and 15.6-fold increases, respectively, in the t1/2 value relative to that of the corresponding wild-type enzyme. The SAP library therefore shows great application potential in stability enhancement of enzymes/proteins." @default.
• W2901364088 created "2018-11-29" @default.
• W2901364088 creator A5004433515 @default.
• W2901364088 creator A5014295844 @default.
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• W2901364088 date "2019-02-01" @default.
• W2901364088 modified "2023-09-27" @default.
• W2901364088 title "An efficient thermostabilization strategy based on self-assembling amphipathic peptides for fusion tags" @default.
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• W2901364088 doi "https://doi.org/10.1016/j.enzmictec.2018.11.004" @default.
• W2901364088 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30554647" @default.
• W2901364088 hasPublicationYear "2019" @default.
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