Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities

Adv Sci (Weinh). 2022 Nov;9(32):e2202359. doi: 10.1002/advs.202202359. Epub 2022 Aug 21.


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.

Keywords: anionization; cationic polymer surfactant; lipase; myoglobin; solvent-free liquid enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hydrolysis
  • Lipase* / chemistry
  • Lipase* / metabolism
  • Myoglobin / chemistry
  • Polymers / chemistry
  • Solvents / chemistry
  • Surface-Active Agents* / chemistry


  • Solvents
  • Lipase
  • Surface-Active Agents
  • Polymers
  • Myoglobin