Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities.
Adv Sci (Weinh)
; 9(32): e2202359, 2022 11.
Article
em En
| MEDLINE
| ID: mdl-35988154
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.
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Bases de dados:
MEDLINE
Assunto principal:
Tensoativos
/
Lipase
Idioma:
En
Revista:
Adv Sci (Weinh)
Ano de publicação:
2022
Tipo de documento:
Article