Abstract
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 language | English |
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Article number | 2202359 |
Journal | Advanced Science |
Volume | 9 |
Issue | 32 |
Number of pages | 9 |
ISSN | 2198-3844 |
DOIs | |
Publication status | Published - 14 Nov 2022 |
Keywords
- anionization
- cationic polymer surfactant
- lipase
- myoglobin
- solvent-free liquid enzyme