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Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities

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  • Ye Zhou, Key Laboratory for Molecular Enzymology and Engineering, School of Life Science, Jilin University, Changchun, China
  • ,
  • Jannik Nedergaard Pedersen
  • ,
  • Jacob Nedergaard Pedersen
  • ,
  • Nykola C. Jones
  • Søren Vrønning Hoffmann
  • Steen Vang Petersen
  • Jan Skov Pedersen
  • Adam Perriman, University of Bristol
  • ,
  • Renjun Gao, Key Laboratory for Molecular Enzymology and Engineering, The Ministry of Education, School of Life Science, Jilin University
  • ,
  • Zheng Guo

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.

OriginalsprogEngelsk
Artikelnummer2202359
TidsskriftAdvanced Science
Vol/bind9
Nummer32
Antal sider9
ISSN2198-3844
DOI
StatusUdgivet - nov. 2022

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