Pressure effects on activity and selectivity of Candida rugosa lipase in organic solvents

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Pressure effects on activity and selectivity of Candida rugosa lipase in organic solvents. / Herbst, Daniela; Peper, Stephanie; Fernández, José Francisco; Ruck, Wolfgang; Niemeyer, Bernd.

in: Journal of Molecular Catalysis B: Enzymatic, Jahrgang 100, 02.2014, S. 104-110.

Publikation: Beiträge in ZeitschriftenZeitschriftenaufsätzeForschungbegutachtet

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@article{e8454c30f57244f8b5cff843cbfe458c,
title = "Pressure effects on activity and selectivity of Candida rugosa lipase in organic solvents",
abstract = "Even though a lot of high pressure studies on enzyme structure, stability and activity are published in the last years, just a few works deal with the influence of pressure on the enantioselectivity of an enzymatic reaction. Furthermore, a change of the reaction medium from buffer to organic solvents for high pressure studies offers some interesting advantages, like pH independency and higher sensitivity towards hydration changes. From this point of view, in the present paper the influence of high pressure on the activity and selectivity of a Candida rugosa Lipase catalyzed reaction in organic solvents was examined. The transesterification of 1-phenylpropan-2-ol with vinyl acetate was chosen as a model reaction. The reactions carried out at 50 MPa showed an increased specific activity of the lipase, independent of solvent composition, reaction temperature and water content of the solvent. An activity maximum, without deactivation, was observed in hexane at 45 C and 200 MPa. Between 50 MPa and 200 MPa a linear increase in the enantiomeric excess (eeR) could be detected, also independent of the solvent composition, reaction temperature and water content of the reaction medium. Furthermore, if additional water was added to the reaction solvent no change of the eeR at high pressures could be observed. This leads to the conclusion that the eeR under pressure is probably mainly influenced by the compression state of the enzyme or by structural changes of the active center rather than by the water content of the enzyme, as it is the case at ambient pressure.",
keywords = "Chemistry, Candida rugosa lipase, Energy research, Enzyme catalysis, High pressure, Organic solvent, Selectivity",
author = "Daniela Herbst and Stephanie Peper and Fern{\'a}ndez, {Jos{\'e} Francisco} and Wolfgang Ruck and Bernd Niemeyer",
year = "2014",
month = feb,
doi = "10.1016/j.molcatb.2013.12.002",
language = "English",
volume = "100",
pages = "104--110",
journal = "Journal of Molecular Catalysis - B Enzymatic",
issn = "1381-1177",
publisher = "Elsevier B.V.",

}

RIS

TY - JOUR

T1 - Pressure effects on activity and selectivity of Candida rugosa lipase in organic solvents

AU - Herbst, Daniela

AU - Peper, Stephanie

AU - Fernández, José Francisco

AU - Ruck, Wolfgang

AU - Niemeyer, Bernd

PY - 2014/2

Y1 - 2014/2

N2 - Even though a lot of high pressure studies on enzyme structure, stability and activity are published in the last years, just a few works deal with the influence of pressure on the enantioselectivity of an enzymatic reaction. Furthermore, a change of the reaction medium from buffer to organic solvents for high pressure studies offers some interesting advantages, like pH independency and higher sensitivity towards hydration changes. From this point of view, in the present paper the influence of high pressure on the activity and selectivity of a Candida rugosa Lipase catalyzed reaction in organic solvents was examined. The transesterification of 1-phenylpropan-2-ol with vinyl acetate was chosen as a model reaction. The reactions carried out at 50 MPa showed an increased specific activity of the lipase, independent of solvent composition, reaction temperature and water content of the solvent. An activity maximum, without deactivation, was observed in hexane at 45 C and 200 MPa. Between 50 MPa and 200 MPa a linear increase in the enantiomeric excess (eeR) could be detected, also independent of the solvent composition, reaction temperature and water content of the reaction medium. Furthermore, if additional water was added to the reaction solvent no change of the eeR at high pressures could be observed. This leads to the conclusion that the eeR under pressure is probably mainly influenced by the compression state of the enzyme or by structural changes of the active center rather than by the water content of the enzyme, as it is the case at ambient pressure.

AB - Even though a lot of high pressure studies on enzyme structure, stability and activity are published in the last years, just a few works deal with the influence of pressure on the enantioselectivity of an enzymatic reaction. Furthermore, a change of the reaction medium from buffer to organic solvents for high pressure studies offers some interesting advantages, like pH independency and higher sensitivity towards hydration changes. From this point of view, in the present paper the influence of high pressure on the activity and selectivity of a Candida rugosa Lipase catalyzed reaction in organic solvents was examined. The transesterification of 1-phenylpropan-2-ol with vinyl acetate was chosen as a model reaction. The reactions carried out at 50 MPa showed an increased specific activity of the lipase, independent of solvent composition, reaction temperature and water content of the solvent. An activity maximum, without deactivation, was observed in hexane at 45 C and 200 MPa. Between 50 MPa and 200 MPa a linear increase in the enantiomeric excess (eeR) could be detected, also independent of the solvent composition, reaction temperature and water content of the reaction medium. Furthermore, if additional water was added to the reaction solvent no change of the eeR at high pressures could be observed. This leads to the conclusion that the eeR under pressure is probably mainly influenced by the compression state of the enzyme or by structural changes of the active center rather than by the water content of the enzyme, as it is the case at ambient pressure.

KW - Chemistry

KW - Candida rugosa lipase

KW - Energy research

KW - Enzyme catalysis

KW - High pressure

KW - Organic solvent

KW - Selectivity

UR - http://www.scopus.com/inward/record.url?scp=84891528844&partnerID=8YFLogxK

U2 - 10.1016/j.molcatb.2013.12.002

DO - 10.1016/j.molcatb.2013.12.002

M3 - Journal articles

AN - SCOPUS:84891528844

VL - 100

SP - 104

EP - 110

JO - Journal of Molecular Catalysis - B Enzymatic

JF - Journal of Molecular Catalysis - B Enzymatic

SN - 1381-1177

ER -

DOI