Lipase-catalyzed synthesis of MPEG methyl acrylates in solvent-free system

Jing Wang; Hanxiao Ying; Jinlian Ma; Xun Cao; Kequan Chen; Jun Ge; Ouyang Pingkai

doi:10.1016/j.molcatb.2015.10.001

Lipase-catalyzed synthesis of MPEG methyl acrylates in solvent-free system

Jing Wang, Hanxiao Ying, Jinlian Ma, Xun Cao, Kequan Chen, Jun Ge, Ouyang Pingkai

COLLEGE OF BIOTECHNOLOGY AND PHARMACEUTICAL ENGINEERING

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

5 Scopus citations

Abstract

The first enzymatic synthesis of the polycarboxylate superplasticizer monomer, MPEG methyl acrylate (MPEGMA) in solvent-free system was established using Novozym 435, an immobilized lipase, as the catalyst, mPEG and methyl acrylic acid (MAA) as the substrates. At the optimal condition, 10% (w/w) enzyme catalyst loading and molar ratio of mPEG to MAA as 1:1, the esterification yield in such solvent-free system at 60 °C reached 76.2%, 1.14-fold higher than that obtained using paraxylene as solvent. A kinetic model for this solvent-free enzymatic synthesis was proposed on the basis of ping-pong bi-bi mechanism and was validated by the good agreement between the predicted data and the experimental results.

Original language	English
Pages (from-to)	305-313
Number of pages	9
Journal	Journal of Molecular Catalysis - B Enzymatic
Volume	122
DOIs	https://doi.org/10.1016/j.molcatb.2015.10.001
State	Published - 1 Dec 2015

Keywords

Enzymatic synthesis
Immobilized enzyme
Lipase
MPEG methyl acrylate (MPEGMA)

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10.1016/j.molcatb.2015.10.001

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title = "Lipase-catalyzed synthesis of MPEG methyl acrylates in solvent-free system",

abstract = "The first enzymatic synthesis of the polycarboxylate superplasticizer monomer, MPEG methyl acrylate (MPEGMA) in solvent-free system was established using Novozym 435, an immobilized lipase, as the catalyst, mPEG and methyl acrylic acid (MAA) as the substrates. At the optimal condition, 10% (w/w) enzyme catalyst loading and molar ratio of mPEG to MAA as 1:1, the esterification yield in such solvent-free system at 60 °C reached 76.2%, 1.14-fold higher than that obtained using paraxylene as solvent. A kinetic model for this solvent-free enzymatic synthesis was proposed on the basis of ping-pong bi-bi mechanism and was validated by the good agreement between the predicted data and the experimental results.",

keywords = "Enzymatic synthesis, Immobilized enzyme, Lipase, MPEG methyl acrylate (MPEGMA)",

author = "Jing Wang and Hanxiao Ying and Jinlian Ma and Xun Cao and Kequan Chen and Jun Ge and Ouyang Pingkai",

year = "2015",

month = dec,

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doi = "10.1016/j.molcatb.2015.10.001",

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volume = "122",

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journal = "Journal of Molecular Catalysis - B Enzymatic",

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TY - JOUR

T1 - Lipase-catalyzed synthesis of MPEG methyl acrylates in solvent-free system

AU - Wang, Jing

AU - Ying, Hanxiao

AU - Ma, Jinlian

AU - Cao, Xun

AU - Chen, Kequan

AU - Ge, Jun

AU - Pingkai, Ouyang

PY - 2015/12/1

Y1 - 2015/12/1

N2 - The first enzymatic synthesis of the polycarboxylate superplasticizer monomer, MPEG methyl acrylate (MPEGMA) in solvent-free system was established using Novozym 435, an immobilized lipase, as the catalyst, mPEG and methyl acrylic acid (MAA) as the substrates. At the optimal condition, 10% (w/w) enzyme catalyst loading and molar ratio of mPEG to MAA as 1:1, the esterification yield in such solvent-free system at 60 °C reached 76.2%, 1.14-fold higher than that obtained using paraxylene as solvent. A kinetic model for this solvent-free enzymatic synthesis was proposed on the basis of ping-pong bi-bi mechanism and was validated by the good agreement between the predicted data and the experimental results.

AB - The first enzymatic synthesis of the polycarboxylate superplasticizer monomer, MPEG methyl acrylate (MPEGMA) in solvent-free system was established using Novozym 435, an immobilized lipase, as the catalyst, mPEG and methyl acrylic acid (MAA) as the substrates. At the optimal condition, 10% (w/w) enzyme catalyst loading and molar ratio of mPEG to MAA as 1:1, the esterification yield in such solvent-free system at 60 °C reached 76.2%, 1.14-fold higher than that obtained using paraxylene as solvent. A kinetic model for this solvent-free enzymatic synthesis was proposed on the basis of ping-pong bi-bi mechanism and was validated by the good agreement between the predicted data and the experimental results.

KW - Enzymatic synthesis

KW - Immobilized enzyme

KW - Lipase

KW - MPEG methyl acrylate (MPEGMA)

UR - http://www.scopus.com/inward/record.url?scp=84946905813&partnerID=8YFLogxK

U2 - 10.1016/j.molcatb.2015.10.001

DO - 10.1016/j.molcatb.2015.10.001

M3 - 文章

AN - SCOPUS:84946905813

SN - 1381-1177

VL - 122

SP - 305

EP - 313

JO - Journal of Molecular Catalysis - B Enzymatic

JF - Journal of Molecular Catalysis - B Enzymatic

ER -

Lipase-catalyzed synthesis of MPEG methyl acrylates in solvent-free system

Abstract

Keywords

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