Improving the organic solvent resistance of lipase a from Bacillus subtilis in water–ethanol solvent through rational surface engineering

Kyoungseon Min; Hee Taek Kim; Si Jae Park; Siseon Lee; Ye Jean Jung; Jin Suk Lee; Young Je Yoo; Jeong Chan Joo

doi:10.1016/j.biortech.2021.125394

Improving the organic solvent resistance of lipase a from Bacillus subtilis in water–ethanol solvent through rational surface engineering

Kyoungseon Min, Hee Taek Kim, Si Jae Park, Siseon Lee, Ye Jean Jung, Jin Suk Lee, Young Je Yoo, Jeong Chan Joo

Department of Chemical Engineering & Materials Science

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

Given that lipase is an enzyme applicable in various industrial fields and water-miscible organic solvents are important reaction media for developing industrial-scale biocatalysis, a structure-based strategy was explored to stabilize lipase A from Bacillus subtilis in a water–ethanol cosolvent. Site-directed mutagenesis of ethanol-interacting sites resulted in 4 mutants, i.e., Ser16Gly, Ala38Gly, Ala38Thr, and Leu108Asn, which were stable in 50% ethanol and had up to 1.8-fold higher stability than the wild-type. In addition, Leu108Asn was more thermostable at 45 °C than the wild type. The results discussed in this study not only provide insights into strategies for enzyme engineering to improve organic solvent resistance but also suggest perspectives on pioneering routes for constructing enzyme-based biorefineries to produce value-added fuels and chemicals.

Original language	English
Article number	125394
Journal	Bioresource Technology
Volume	337
DOIs	https://doi.org/10.1016/j.biortech.2021.125394
State	Published - Oct 2021

Bibliographical note

Publisher Copyright:
© 2021 Elsevier Ltd

Keywords

Bacillus subtilis lipase A
Engineering ethanol-interacting residues
Rational surface design
Stability in water–ethanol cosolvent

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title = "Improving the organic solvent resistance of lipase a from Bacillus subtilis in water–ethanol solvent through rational surface engineering",

abstract = "Given that lipase is an enzyme applicable in various industrial fields and water-miscible organic solvents are important reaction media for developing industrial-scale biocatalysis, a structure-based strategy was explored to stabilize lipase A from Bacillus subtilis in a water–ethanol cosolvent. Site-directed mutagenesis of ethanol-interacting sites resulted in 4 mutants, i.e., Ser16Gly, Ala38Gly, Ala38Thr, and Leu108Asn, which were stable in 50% ethanol and had up to 1.8-fold higher stability than the wild-type. In addition, Leu108Asn was more thermostable at 45 °C than the wild type. The results discussed in this study not only provide insights into strategies for enzyme engineering to improve organic solvent resistance but also suggest perspectives on pioneering routes for constructing enzyme-based biorefineries to produce value-added fuels and chemicals.",

keywords = "Bacillus subtilis lipase A, Engineering ethanol-interacting residues, Rational surface design, Stability in water–ethanol cosolvent",

author = "Kyoungseon Min and Kim, {Hee Taek} and Park, {Si Jae} and Siseon Lee and Jung, {Ye Jean} and Lee, {Jin Suk} and Yoo, {Young Je} and Joo, {Jeong Chan}",

note = "Publisher Copyright: {\textcopyright} 2021 Elsevier Ltd",

year = "2021",

month = oct,

doi = "10.1016/j.biortech.2021.125394",

language = "English",

volume = "337",

journal = "Bioresource Technology",

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T1 - Improving the organic solvent resistance of lipase a from Bacillus subtilis in water–ethanol solvent through rational surface engineering

AU - Min, Kyoungseon

AU - Kim, Hee Taek

AU - Park, Si Jae

AU - Lee, Siseon

AU - Jung, Ye Jean

AU - Lee, Jin Suk

AU - Yoo, Young Je

AU - Joo, Jeong Chan

PY - 2021/10

Y1 - 2021/10

N2 - Given that lipase is an enzyme applicable in various industrial fields and water-miscible organic solvents are important reaction media for developing industrial-scale biocatalysis, a structure-based strategy was explored to stabilize lipase A from Bacillus subtilis in a water–ethanol cosolvent. Site-directed mutagenesis of ethanol-interacting sites resulted in 4 mutants, i.e., Ser16Gly, Ala38Gly, Ala38Thr, and Leu108Asn, which were stable in 50% ethanol and had up to 1.8-fold higher stability than the wild-type. In addition, Leu108Asn was more thermostable at 45 °C than the wild type. The results discussed in this study not only provide insights into strategies for enzyme engineering to improve organic solvent resistance but also suggest perspectives on pioneering routes for constructing enzyme-based biorefineries to produce value-added fuels and chemicals.

AB - Given that lipase is an enzyme applicable in various industrial fields and water-miscible organic solvents are important reaction media for developing industrial-scale biocatalysis, a structure-based strategy was explored to stabilize lipase A from Bacillus subtilis in a water–ethanol cosolvent. Site-directed mutagenesis of ethanol-interacting sites resulted in 4 mutants, i.e., Ser16Gly, Ala38Gly, Ala38Thr, and Leu108Asn, which were stable in 50% ethanol and had up to 1.8-fold higher stability than the wild-type. In addition, Leu108Asn was more thermostable at 45 °C than the wild type. The results discussed in this study not only provide insights into strategies for enzyme engineering to improve organic solvent resistance but also suggest perspectives on pioneering routes for constructing enzyme-based biorefineries to produce value-added fuels and chemicals.

KW - Bacillus subtilis lipase A

KW - Engineering ethanol-interacting residues

KW - Rational surface design

KW - Stability in water–ethanol cosolvent

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DO - 10.1016/j.biortech.2021.125394

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SN - 0960-8524

VL - 337

JO - Bioresource Technology

JF - Bioresource Technology

M1 - 125394

ER -

Improving the organic solvent resistance of lipase a from Bacillus subtilis in water–ethanol solvent through rational surface engineering

Abstract

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Keywords

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