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
N1 - Publisher Copyright:
© 2015 Elsevier B.V. All rights reserved.
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 -