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Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities.


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.

SUBMITTER: Zhou Y 

PROVIDER: S-EPMC9661855 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature

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Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities.

Zhou Ye Y   Pedersen Jannik Nedergaard JN   Pedersen Jacob Nedergaard JN   Jones Nykola C NC   Hoffmann Søren Vrønning SV   Petersen Steen Vang SV   Pedersen Jan Skov JS   Perriman Adam A   Gao Renjun R   Guo Zheng Z  

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 20220821 32


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  ...[more]

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