Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities

Ye Zhou; Jannik Nedergaard Pedersen; Jacob Nedergaard Pedersen; Nykola C. Jones; Søren Vrønning Hoffmann; Steen Vang Petersen; Jan Skov Pedersen; Adam Perriman; Renjun Gao; Zheng Guo

doi:10.1002/advs.202202359

Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities

Ye Zhou, Jannik Nedergaard Pedersen, Jacob Nedergaard Pedersen, Nykola C. Jones, Søren Vrønning Hoffmann, Steen Vang Petersen, Jan Skov Pedersen, Adam Perriman, Renjun Gao^*, Zheng Guo

^*Corresponding author af dette arbejde

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

1 Citationer (Scopus)

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.

Originalsprog	Engelsk
Artikelnummer	2202359
Tidsskrift	Advanced Science
Vol/bind	9
Nummer	32
Antal sider	9
ISSN	2198-3844
DOI	https://doi.org/10.1002/advs.202202359
Status	Udgivet - nov. 2022

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10.1002/advs.202202359Licens: CC BY

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@article{8db2745453aa41a2b258401116d4de19,

title = "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.",

keywords = "anionization, cationic polymer surfactant, lipase, myoglobin, solvent-free liquid enzyme",

author = "Ye Zhou and Pedersen, {Jannik Nedergaard} and Pedersen, {Jacob Nedergaard} and Jones, {Nykola C.} and Hoffmann, {S{\o}ren Vr{\o}nning} and Petersen, {Steen Vang} and Pedersen, {Jan Skov} and Adam Perriman and Renjun Gao and Zheng Guo",

year = "2022",

month = nov,

doi = "10.1002/advs.202202359",

language = "English",

volume = "9",

journal = "Advanced Science",

issn = "2198-3844",

publisher = "Wiley",

number = "32",

}

TY - JOUR

T1 - Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities

AU - Zhou, Ye

AU - Pedersen, Jannik Nedergaard

AU - Pedersen, Jacob Nedergaard

AU - Jones, Nykola C.

AU - Hoffmann, Søren Vrønning

AU - Petersen, Steen Vang

AU - Pedersen, Jan Skov

AU - Perriman, Adam

AU - Gao, Renjun

AU - Guo, Zheng

PY - 2022/11

Y1 - 2022/11

N2 - 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.

AB - 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.

KW - anionization

KW - cationic polymer surfactant

KW - lipase

KW - myoglobin

KW - solvent-free liquid enzyme

U2 - 10.1002/advs.202202359

DO - 10.1002/advs.202202359

M3 - Journal article

C2 - 35988154

SN - 2198-3844

VL - 9

JO - Advanced Science

JF - Advanced Science

IS - 32

M1 - 2202359

ER -

Superanionic Solvent-Free Liquid Enzymes Exhibit Enhanced Structures and Activities

Abstract

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