4.8 Article

Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities

Journal

ADVANCED SCIENCE
Volume 9, Issue 32, Pages -

Publisher

WILEY
DOI: 10.1002/advs.202202359

Keywords

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

Funding

  1. Chinese Scholarship Council (CSC)
  2. Novo Nordisk Foundation [NNF16OC0021740]
  3. AUFF-NOVA [AUFF-E-2015-FLS-9- 12]

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This study focuses on the anionization of a carboxylate-enriched mutant of Bacillus subtilis lipase A (8M) to produce biofluids with enhanced hydrolytic activity. The resulting biofluids show a 2.5-fold increase in activity compared to those based on anionic polymer surfactants. Additionally, the use of anion-type biofluids with Myoglobin (Mb) is evaluated, revealing partial recovery of the active alpha-helix level in the biofluids. These highly active solvent-free liquid enzymes exhibit increased thermal stability and open up new possibilities in solvent-free liquid protein research.
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 alpha-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.

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