Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities

Ye Zhou, Jannik Nedergaard Pedersen, Jacob Nedergaard Pedersen, Nykola C. Jones, Søren Vrønning Hoffmann, Steen Vang Petersen, Jan Skov Pedersen, Adam Perriman, Renjun Gao*, Zheng Guo

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review


The surface of a carboxylate-enriched octuple mutant of Bacillus subtilis lipase A (8M) is chemically anionized to produce core (8M)-shell (cationic polymer surfactants) bionanoconjugates in protein liquid form, which are termed anion-type biofluids. The resultant lipase biofluids exhibit a 2.5-fold increase in hydrolytic activity when compared with analogous lipase biofluids based on anionic polymer surfactants. In addition, the applicability of the anion-type biofluid using Myoglobin (Mb) that is well studied in anion-type solvent-free liquid proteins is evaluated. Although anionization resulted in the complete unfolding of Mb, the active α-helix level is partially recovered in the anion-type biofluids, and the effect is accentuated in the cation-type Mb biofluids. These highly active anion-type solvent-free liquid enzymes exhibit increased thermal stability and provide a new direction in solvent-free liquid protein research.

Original languageEnglish
Article number2202359
JournalAdvanced Science
Number of pages9
Publication statusPublished - Nov 2022


  • anionization
  • cationic polymer surfactant
  • lipase
  • myoglobin
  • solvent-free liquid enzyme


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