Novel investigation of enzymatic biodiesel reaction by isothermal calorimetry

Lene Fjerbaek Søtoft, Peter Westh, Knud V. Christensen, Birger Norddahl

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Isothermal calorimetry (ITC) was used to investigate solvent-free enzymatic biodiesel production. The transesterification of rapeseed oil with methanol and ethanol was catalyzed by immobilized lipase Novozym 435 at 40 °C. The aim of the study was to determine reaction enthalpy for the enzymatic transesterification and to elucidate the mass transfer and energetic processes taking place. Based on the measured enthalpy and composition change in the system, the heat of reaction at 40 °C for the two systems was determined as −9.8 ± 0.9 kJ/mole biodiesel formed from rapeseed oil and methanol, and −9.3 ± 0.7 kJ/mole when rapeseed oil and ethanol was used. Simple Michaelis–Menten kinetics was not an appropriate choice for describing the kinetics of this heterogeneous system. The experiments demonstrated the possibility of investigating complex reaction mixtures using ITC. Although it is possible to determine thermodynamic properties such as reaction enthalpy and reaction rate, the difficulty in actually measuring the true non-mass-transfer-limited reaction kinetics is exposed by the high time resolution of ITC.

OriginalsprogEngelsk
TidsskriftThermochimica Acta
Vol/bind501
Udgave nummer1-2
Sider (fra-til)84-90
ISSN0040-6031
DOI
StatusUdgivet - 30 mar. 2010

Citer dette

Søtoft, Lene Fjerbaek ; Westh, Peter ; Christensen, Knud V. ; Norddahl, Birger. / Novel investigation of enzymatic biodiesel reaction by isothermal calorimetry. I: Thermochimica Acta. 2010 ; Bind 501, Nr. 1-2. s. 84-90.
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abstract = "Isothermal calorimetry (ITC) was used to investigate solvent-free enzymatic biodiesel production. The transesterification of rapeseed oil with methanol and ethanol was catalyzed by immobilized lipase Novozym 435 at 40 °C. The aim of the study was to determine reaction enthalpy for the enzymatic transesterification and to elucidate the mass transfer and energetic processes taking place. Based on the measured enthalpy and composition change in the system, the heat of reaction at 40 °C for the two systems was determined as −9.8 ± 0.9 kJ/mole biodiesel formed from rapeseed oil and methanol, and −9.3 ± 0.7 kJ/mole when rapeseed oil and ethanol was used. Simple Michaelis–Menten kinetics was not an appropriate choice for describing the kinetics of this heterogeneous system. The experiments demonstrated the possibility of investigating complex reaction mixtures using ITC. Although it is possible to determine thermodynamic properties such as reaction enthalpy and reaction rate, the difficulty in actually measuring the true non-mass-transfer-limited reaction kinetics is exposed by the high time resolution of ITC.",
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Novel investigation of enzymatic biodiesel reaction by isothermal calorimetry. / Søtoft, Lene Fjerbaek; Westh, Peter; Christensen, Knud V.; Norddahl, Birger.

I: Thermochimica Acta, Bind 501, Nr. 1-2, 30.03.2010, s. 84-90.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Novel investigation of enzymatic biodiesel reaction by isothermal calorimetry

AU - Søtoft, Lene Fjerbaek

AU - Westh, Peter

AU - Christensen, Knud V.

AU - Norddahl, Birger

PY - 2010/3/30

Y1 - 2010/3/30

N2 - Isothermal calorimetry (ITC) was used to investigate solvent-free enzymatic biodiesel production. The transesterification of rapeseed oil with methanol and ethanol was catalyzed by immobilized lipase Novozym 435 at 40 °C. The aim of the study was to determine reaction enthalpy for the enzymatic transesterification and to elucidate the mass transfer and energetic processes taking place. Based on the measured enthalpy and composition change in the system, the heat of reaction at 40 °C for the two systems was determined as −9.8 ± 0.9 kJ/mole biodiesel formed from rapeseed oil and methanol, and −9.3 ± 0.7 kJ/mole when rapeseed oil and ethanol was used. Simple Michaelis–Menten kinetics was not an appropriate choice for describing the kinetics of this heterogeneous system. The experiments demonstrated the possibility of investigating complex reaction mixtures using ITC. Although it is possible to determine thermodynamic properties such as reaction enthalpy and reaction rate, the difficulty in actually measuring the true non-mass-transfer-limited reaction kinetics is exposed by the high time resolution of ITC.

AB - Isothermal calorimetry (ITC) was used to investigate solvent-free enzymatic biodiesel production. The transesterification of rapeseed oil with methanol and ethanol was catalyzed by immobilized lipase Novozym 435 at 40 °C. The aim of the study was to determine reaction enthalpy for the enzymatic transesterification and to elucidate the mass transfer and energetic processes taking place. Based on the measured enthalpy and composition change in the system, the heat of reaction at 40 °C for the two systems was determined as −9.8 ± 0.9 kJ/mole biodiesel formed from rapeseed oil and methanol, and −9.3 ± 0.7 kJ/mole when rapeseed oil and ethanol was used. Simple Michaelis–Menten kinetics was not an appropriate choice for describing the kinetics of this heterogeneous system. The experiments demonstrated the possibility of investigating complex reaction mixtures using ITC. Although it is possible to determine thermodynamic properties such as reaction enthalpy and reaction rate, the difficulty in actually measuring the true non-mass-transfer-limited reaction kinetics is exposed by the high time resolution of ITC.

KW - ITC

KW - Biodiesel

KW - Enzyme

KW - Lipase

KW - Transesterification

KW - Reaction enthalpy

U2 - 10.1016/j.tca.2010.01.014

DO - 10.1016/j.tca.2010.01.014

M3 - Journal article

VL - 501

SP - 84

EP - 90

JO - Thermochimica Acta

JF - Thermochimica Acta

SN - 0040-6031

IS - 1-2

ER -