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Søren Vrønning Hoffmann

Insight into the structure and activity of surface-engineered lipase biofluids

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Insight into the structure and activity of surface-engineered lipase biofluids. / Zhou, Ye; Jones, Nykola C.; Pedersen, Jannik Nedergaard; Perez, Bianca; Hoffmann, Søren Vrønning; Petersen, Steen Vang; Pedersen, Jan Skov; Perriman, Adam; Kristensen, Peter; Gao, Renjun; Guo, Zheng.

I: ChemBioChem, Bind 20, Nr. 10, 05.2019, s. 1266-1272.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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@article{26004263168d429da1adcef35714f918,
title = "Insight into the structure and activity of surface-engineered lipase biofluids",
abstract = "Despite a successful application of solvent-free liquid protein (biofluids) concept to a number of commercial enzymes, the technical advantages of enzyme biofluids as hyperthermal stable biocatalysts cannot be fully utilized as up to 90–99% of native activities are lost when enzymes were made into biofluids. With a two-step strategy (site-directed mutagenesis and synthesis of variant biofluids) on Bacillus subtilis lipase A (BsLA), we elucidated a strong dependency of structure and activity on the number and distribution of polymer surfactant binding sites on BsLA surface. Here, it is demonstrated that improved BsLA variants can be engineered via site-mutagenesis by a rational design, either with enhanced activity in aqueous solution in native form, or with improved physical property and increased activity in solvent-free system in the form of a protein liquid. This work answered some fundamental questions about the surface characteristics for construction of biofluids, useful for identifying new strategies for developing advantageous biocatalysts.",
keywords = "lipases, mutagenesis, nanostructures, polymer surfactants, protein engineering, STABILITY, FREE PROTEIN LIQUIDS, BACILLUS-SUBTILIS LIPASE",
author = "Ye Zhou and Jones, {Nykola C.} and Pedersen, {Jannik Nedergaard} and Bianca Perez and Hoffmann, {S{\o}ren Vr{\o}nning} and Petersen, {Steen Vang} and Pedersen, {Jan Skov} and Adam Perriman and Peter Kristensen and Renjun Gao and Zheng Guo",
year = "2019",
month = may,
doi = "10.1002/cbic.201800819",
language = "English",
volume = "20",
pages = "1266--1272",
journal = "ChemBioChem",
issn = "1439-4227",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "10",

}

RIS

TY - JOUR

T1 - Insight into the structure and activity of surface-engineered lipase biofluids

AU - Zhou, Ye

AU - Jones, Nykola C.

AU - Pedersen, Jannik Nedergaard

AU - Perez, Bianca

AU - Hoffmann, Søren Vrønning

AU - Petersen, Steen Vang

AU - Pedersen, Jan Skov

AU - Perriman, Adam

AU - Kristensen, Peter

AU - Gao, Renjun

AU - Guo, Zheng

PY - 2019/5

Y1 - 2019/5

N2 - Despite a successful application of solvent-free liquid protein (biofluids) concept to a number of commercial enzymes, the technical advantages of enzyme biofluids as hyperthermal stable biocatalysts cannot be fully utilized as up to 90–99% of native activities are lost when enzymes were made into biofluids. With a two-step strategy (site-directed mutagenesis and synthesis of variant biofluids) on Bacillus subtilis lipase A (BsLA), we elucidated a strong dependency of structure and activity on the number and distribution of polymer surfactant binding sites on BsLA surface. Here, it is demonstrated that improved BsLA variants can be engineered via site-mutagenesis by a rational design, either with enhanced activity in aqueous solution in native form, or with improved physical property and increased activity in solvent-free system in the form of a protein liquid. This work answered some fundamental questions about the surface characteristics for construction of biofluids, useful for identifying new strategies for developing advantageous biocatalysts.

AB - Despite a successful application of solvent-free liquid protein (biofluids) concept to a number of commercial enzymes, the technical advantages of enzyme biofluids as hyperthermal stable biocatalysts cannot be fully utilized as up to 90–99% of native activities are lost when enzymes were made into biofluids. With a two-step strategy (site-directed mutagenesis and synthesis of variant biofluids) on Bacillus subtilis lipase A (BsLA), we elucidated a strong dependency of structure and activity on the number and distribution of polymer surfactant binding sites on BsLA surface. Here, it is demonstrated that improved BsLA variants can be engineered via site-mutagenesis by a rational design, either with enhanced activity in aqueous solution in native form, or with improved physical property and increased activity in solvent-free system in the form of a protein liquid. This work answered some fundamental questions about the surface characteristics for construction of biofluids, useful for identifying new strategies for developing advantageous biocatalysts.

KW - lipases

KW - mutagenesis

KW - nanostructures

KW - polymer surfactants

KW - protein engineering

KW - STABILITY

KW - FREE PROTEIN LIQUIDS

KW - BACILLUS-SUBTILIS LIPASE

U2 - 10.1002/cbic.201800819

DO - 10.1002/cbic.201800819

M3 - Journal article

C2 - 30624001

VL - 20

SP - 1266

EP - 1272

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

IS - 10

ER -