Solvent-free biocatalytic interesterification of acrylate derivatives

Article abstract of DOI:10.1016/j.cattod.2012.02.055

The ability of diverse commercial lipases and whole cells (fungal resting cells) to synthesise allyl and dichloropropyl acrylate from allyl dodecanoate through an interesterification process is presented. The process was carried out without solvent in a conventional batch system. The best biocatalyst among those studied was the commercial enzyme CALB (Candida antarctica lipase B immobilised onto a macroporous acrylic resin). The reaction was sensitive to water activity, and a decrease in the yield was observed at the highest activity studied. CALB could also be applied to diverse acrylic derivatives, although the yields decreased using either ethyl methacrylate or acrylic acid.

Full text of DOI:10.1016/j.cattod.2012.02.055

Catalysis Today 196 (2012) 86–90
Contents lists available at SciVerse ScienceDirect
Catalysis Today
journal homepage: www.elsevier.com/locate/cattod
Solvent-free biocatalytic interesterification of acrylate derivatives
Edinson Yara-Varóna, Jordi Eras Jolia,∗, Mercè Torresb, Nuria Salab, Gemma Villorbinaa,
Jonh Jairo Méndezc, Ramon Canela-Garayoaa,∗∗
a Department of Chemistry, University of Lleida, Plac¸ a Víctor Siurana 1, Lleida, Spain
b Department of Food Science and Technology, University of Lleida, Plac¸ a Víctor Siurana 1, Lleida, Spain
c Department of Chemistry, University of the Tolima, Barrio S. Helena, Ibague, Colombia
a r t i c l e i n f o
a b s t r a c t
Article history:
The ability of diverse commercial lipases and whole cells (fungal resting cells) to synthesise allyl and
dichloropropyl acrylate from allyl dodecanoate through an interesterification process is presented. The
process was carried out without solvent in a conventional batch system. The best biocatalyst among those
studied was the commercial enzyme CALB (Candida antarctica lipase B immobilised onto a macroporous
acrylic resin). The reaction was sensitive to water activity, and a decrease in the yield was observed at
the highest activity studied. CALB could also be applied to diverse acrylic derivatives, although the yields
decreased using either ethyl methacrylate or acrylic acid.
Received 28 October 2011
Received in revised form 24 February 2012
Accepted 27 February 2012
Available online 8 April 2012
Keywords:
Biocatalytic interesterification
Acrylate derivatives
CALB
© 2012 Elsevier B.V. All rights reserved.
Resting cells
Water activity
Solvent-free
1. Introduction
On the other hand, the implementation of green chemistry
requires the discovery and development of new synthetic path-
Acrylic acid and its esters are frequently used as monomers
for the production of polymers and copolymers of commercial
interest. These materials have applications in the production of
dyes, paper, textiles, glues, adhesives, binders, paints, dispersants,
thickeners, and flocculants. Allyl acrylate is widely produced in
addition to methyl, ethyl, n-butyl, and 2-ethylhexyl acrylates [1–5].
Chlorohydrin acrylates are putative monomers used to prepare
functionalised polyacrylates.
Whereas the synthesis of chlorohydrin acrylates has not been
described as far as we know, allyl acrylate is usually prepared by the
esterification of acrylic acid or some derivatives with allyl alcohol
[6] or allyl bromide [7]. This process can be carried out in differ-
ent ways, using an alkali or acid catalyst [8–10]. However, chemical
catalysis requires the use of special operating procedures and poly-
merisation inhibitors to avoid undesired reactions. Although these
chemical processes are used on an industrial scale, the reaction has
several drawbacks: it is energy intensive, the acidic or alkaline cata-
lyst has to be removed from the product, and the non-neutral waste
water requires treatment.
ways using alternative feedstocks, improved reaction conditions,
catalysts for improved selectivity and energy minimisation, and the
design of environmentally compatible processes. These new tech-
niques are urgently required to overcome many of the bottlenecks
associated with conventional organic synthesis.
Enzymatic catalysis presents advantages over chemical catalysts
with milder reaction conditions, greater specificity, high stabil-
ity, high selectivity with fewer by-products, wide sources, and a
broad range of substrates [11,12]. Biocatalysis is considered an
environmentally benign alternative to chemical transformations.
Reactions can be carried out in organic solvents or in solvent-free
processes [13–15]. The solvent-free processes are considered more
environment-friendly with the additional advantages of a more
volume-efficient reactor [16]. The use of hydrolases, especially
lipases, has expanded rapidly in recent years. Lipases (EC 3.1.1.3)
may catalyse different reactions such as hydrolysis, esterification,
transesterification, and interesterification and play an important
role in industrial production [17–20]. They have been used to pre-
pare diverse alkyl acrylates by the esterification of acrylic acid or
the transacylation of methyl acrylates using diverse alcohols [21].
Recently, we have described the synthesis of chlorohydrin esters
using glycerol and carboxylic acids. These esters can be transformed
into allyl esters avoiding the use of the harmful allyl alcohol [22].
Crude glycerol from the biodiesel industry and vegetable oils or
fat from agrofood wastes can also be used as starting materials to
∗
Corresponding author. Tel.: +34 973 702589; fax: +34 973 238264.
Corresponding author. Tel.: +34 973 702843; fax: +34 973238264.
E-mail addresses: eras@quimica.udl.cat (J. Eras Joli), canela@quimica.udl.cat (R.
∗∗
Canela-Garayoa).
0920-5861/$ – see front matter © 2012 Elsevier B.V. All rights reserved.
doi:10.1016/j.cattod.2012.02.055

E. Yara-Varón et al. / Catalysis Today 196 (2012) 86–90
87
obtain both esters [23]. Consequently, we dispose of a new source of
chlorohydrin and allyl derivatives from renewable sources, which
may be used to prepare valuable compounds. For instance, they
could be used in interesterification reactions, thus diminishing
the possibility of enzyme inhibition provoked by diverse alcohols
[24,25]. Interesterification processes have been extensively used to
modify triacylglycerides [26–28].
The aim of this study was to present the results obtained using
diverse commercial lipases and whole cells (fungal resting cells)
for synthesising allyl and chlorohydrin acrylates using allyl and
dichloropropyl dodecanoates through an interesterification pro-
cess. The solvent-free process was carried out in a conventional
batch system.
was stirred (1200 rpm) continuously at atmospheric pressure in
a reaction vial (1.5 mL) fitted with a PTFE-lined cap. Two sets of
experiments were carried out using either 3.3% or 15% (w/w) of
a biocatalyst based on the weight of allyl or dichloropropyl dode-
canoate. Samples were collected after a given time, depending on
the experiment carried out. The reaction temperature was cho-
sen considering the previously described optimum temperature
for each commercial enzyme. For resting cells, the temperature
used was 40 ◦C. Once the experiment was concluded, an aliquot
of 10 mg of the crude material of the reaction was dissolved in hex-
ane containing an internal standard (typically butyl acrylate). The
resulting solution was analysed using gas chromatography (GC-
FID). Quantification of each compound was carried out using the
corresponding internal standard. Experiments were carried out in
triplicate.
2. Experimental
Using the same procedure, the reaction was used to study the
effect of an excess of either allyl or dichloropropyl dodecanoates on
the allyl or dichloropropyl acrylate yields, respectively. The ratio
was set at 1:5 ethyl acrylate to dodecanoate esters.
2.1. Enzymes and chemicals
Candida antarctica lipase B immobilised onto a macroporous
acrylic resin (CALB), Amano lipase PS-IM immobilised on diatoma-
ceous earth (PS-IM), lipase immobilised on Immobead 150 from
Rhizopus oryzae (IM-150), lipozyme immobilised from Mucor miehei
(MmL2), and dodecanoic acid were purchased from Sigma. Ethyl
dodecanoate, allyl methacrylate, ethyl methacrylate, acrylic acid,
Amano lipase PS (Burkhloderia cepacia) (PsL), Amano lipase A from
Aspergillus niger (AnLA), and Amano lipase AYS from Candida rugosa
(AYSL) were purchased from Aldrich. Ethyl acrylate, butyl acry-
late, lipase from C. rugosa (CrL), and Lipozyme immobilised from M.
miehei (MmL1) were purchased from Fluka (Sigma–Aldrich Quim-
ica, S.A., Madrid, Spain). Allyl acrylate was purchased from Alfa
Aesar (Barcelona, Spain) and hexane was purchased from J.T. Baker
(Quimega, Lleida, Spain).
2.5. Equilibration of water activity
The water activity (aw) in the experiments was set by equilibrat-
ing reagents (ethyl acrylate and allyl dodecanoate, independently)
and CALB with aqueous saturated solutions of MgCl2. Separate ves-
sels were used for each reactant and enzyme [33]. Equilibration was
performed at the reaction temperature (50 ◦C) for 16 h. The water
activity was measured using an Aqua Lab series 3TE from Decagon
Devices Inc. (Pullman, WA, USA).
2.6. Gas chromatography analysis
The progress of each reaction was determined by gas chro-
matography using an Agilent (Barcelona, Spain) HP6890 series
GC coupled to a FID detector. The analytical column was a
30 m × 0.25 mm fused silica capillary coated with a 0.20 ␮m film
of poly(80% biscyanopropyl-20% cyanopropylphenyl siloxane) (SP-
2330; Supelco, Madrid, Spain). The temperature programme used
was 40 ◦C for 5 min, then the temperature was increased to 225 ◦C
at a heating rate of 20 ◦C/min, and then to 225 ◦C at a heating rate
of 3 ◦C/min. A 1:20 split injection ratio was used. Hydrogen was
employed as the carrier gas at constant pressure of 620 kPa. The
injection volume was 1 ␮L. The injection system was held at 250 ◦C
and the FID system was held at 280 ◦C. Quantification was carried
out by a conventional internal standard calibration method using
the corresponding acrylic ester standards.
2.2. Procedure for obtaining resting cells
The strain of R. oryzae 1 used in this work was isolated from
Foeniculum vulgare as endophytic fungi [29] and the other fungal
mycelia (R. oryzae 2 and 3, A. fumigatus, A. flavus and A. niger) were
isolated from the soil of olive (Olea europaea) orchards.
The fungal strains were cultivated in a synthetic liquid medium
as previously described [30]. Mycelia were harvested from the
whole culture broth by filtration using a Buchner funnel and
washed with distilled water followed by acetone. The mycelia were
dried under vacuum for 18 h and ground into a powder [31,32].
The enzymatic units (U) were determined for each of resting cells
considering the enzymatic hydrolysis rate of methyl stearate. U cor-
responds to the amount of enzyme needed to hydrolise 1 ␮mol of
stearic acid per min at 40 ◦C. The specific activity of fungal resting
cells was calculated by U/m, where m is the amount of resting cell
measured in g.
3. Results and discussion
The solvent-free reactions were carried out using an equimo-
lar ratio of allyl dodecanoate and ethyl acrylate. Fifteen diverse
biocatalysts were used as putative catalysts for the interesterifica-
tion reaction. Nine of them were commercially available lipases, of
which five were immobilised on polymeric supports and four were
in powder form. The other six were resting cells. The resting cells
were obtained in our laboratory by lyophilising fungal mycelia pre-
senting lipase activity. Two different percentages of biocatalysts,
3.3% and 15% (w/w), were used. Samples were taken at 1 h and
the amounts of allyl and ethyl acrylates were determined by GC.
Table 1 shows that four of the five supported catalysts were able
to catalyse the interesterification reaction to some extent. Among
them, IM-150 was the only one which did not show biocatalyst
concentration dependence. Curiously, one Lipozyme from M. miehei
(MmL2) did not present any activity, whereas MmL1 showed yields
closer to that of PS-IM. Apart from the supplier, the only difference
described by the dealers for MmL1 and MmL2 was the Enzymatic
2.3. Procedure for the preparation allyl and dichloropropyl
dodecanoates
Allyl and dichloropropyl dodecanoates were prepared from
dodecanoic acid according to a previously described process [23].
The crude material of allyl dodecanoate synthesis was purified
by distillation under vacuum using a Buchi Kugelrohr apparatus
(Massó Analítica S.A., Barcelona, Spain). Finally, the crude mate-
rial of dichloropropyl dodecanoate synthesis was purified by SiO2
column chromatography.
2.4. Enzymatic interesterification
For the standard reaction, a 1:1 mixture of ethyl acrylate
and either allyl or dichloropropyl dodecanoates (1 mmol each)

88
E. Yara-Varón et al. / Catalysis Today 196 (2012) 86–90
Table 1
Percentage of allyl acrylate obtained using diverse commercial enzymes and resting cells with lipase activity. Reaction time 1 h.
Biocatalyst
Biocatalyst support
Specific activitya (U, g × 103)
Temperature (◦C)
Yield (%)
Biocatalyst concentration
(%w/w)b
3.3
15
CALB
PS-IM
MmL 1
MmL 2
IM-150
AnLA
PsL
AYSL
CrL
R. oryzae (1)
R. oryzae (2)
R. oryzae (3)
A. niger
A. fumigatus
A. flavus
Acrylic resin
111
0.943
0.140
0.110
0.367
129
50
50
50
50
40
45
50
40
45
40
40
40
40
40
40
20.5 0.1
4.8 0.1
4.9 0.0
–
45.5 0.1
7.6 0.5
7.1 0.2
–
4.5 0.0
–
7.2 0.0
–
Diatomaceous earth
Ion-exchange resin
Ion-exchange resin
Immobead 150
Powder, free enzyme
Powder, free enzyme
Powder, free enzyme
Powder, free enzyme
Resting cells
Resting cells
Resting cells
Resting cells
Resting cells
4.5 0.0
–
–
–
–
–
–
–
–
–
–
34.5
31600
0.0029
190
54
6340
234
–
–
–
2.1 0.1
–
7.6 0.2
7.7 0.1
175
118
Resting cells
a
Specific activity of commercial enzyme provided by the supplier and calculated experimentally for resting cells.
Based on the weight of allyl dodecanoate.
b
Units, showing that MmL1 was 22% more active than MmL2. Only
first assayed reaction. Moreover, in this case, MmL1 gave much
closer yields to those obtained with CALB. These results can be
explained by the fact that the alkanol residue with dichloropropyl
esters is a secondary alcohol whereas allyl alcohol is a primary
alcohol.
CALB supported on acrylic resin (also known as Novozyme 435)
has already been described as the best catalyst to prepare octyl
acrylate from acrylic acid and 1-octanol [21]. The reaction was
carried out in an organic solvent and the yield was moisture-
dependent.
Considering these results, a new set of experiments was car-
ried out using the three commercial supported enzymes showing
the best conversion ratio for allyl dodecanoate in the 3.3% and 15%
experiments. The new experiments were carried out for 24 h and
samples were taken at various time intervals. Fig. 1 shows that CALB
was superior in terms of the reaction rate and conversion through-
out the 24 h study. Using 3.3% biocatalyst, CALB was able to convert
up to 45% of ethyl acrylate to allyl acrylate after 6 h of reaction,
whereas the other two biocatalysts were only able to yield conver-
sions around 10% after 24 h of reaction (Fig. 1A). Using 15% (w/w)
biocatalyst, CALB gave similar conversions after 1 h of reaction.
Although after 24 h of reaction MmL1 showed conversions closer to
those of CALB, this enzyme still showed a lower reaction rate than
CALB. PS-IM was the worst among the three biocatalysts studied. It
yielded conversions up to 30% after 24 h of reaction (Fig. 1, graphic
B). Although 45% was the best percentage reached, the final mix-
ture could be useful to prepare copolymers of diverse alkyl acrylates
[35].
R. oryzae 3, among the three resting cells prepared from different
R. oryzae strains, was able to transform in a moderate way ethyl
acrylate to allyl acrylate (2.13% yield using 15% biocatalyst). Two
resting cells, A. fumigatus and A. flavus, showed better results than
R. oryzae. These yields were similar to PsL (around 7% using 15% bio-
catalyst), whereas A. niger did not present any activity. Apart from
PsL, none of the other powdered commercial enzymes were able
to carry out the desired interesterification reaction to any extent.
Without any doubt, C. antarctica lipase B (CALB) was the best bio-
catalyst for carrying out this reaction considering that the same
amount of catalyst was used in all the experiments. These results
are in spite of that the specific activity of the CALB not was the
best among all the biocatalysts assayed (see Table 1). These results
are similar to those described by Warwel et al. [34] which showed
that CALB (also known as Pseudozyma antarctica lipase B, EC 3.1.1.3)
was a superior catalyst out of 19 enzymes investigated in the bio-
catalysed transacylation of methyl acrylate with 1-undecanol. This
reaction was also carried out in a solvent-free system. Neverthe-
less, the molar ratio of acrylate ester to 1-undecanol was 90:1 in
this case.
Those biocatalysts that showed some activity in transform-
ing ethyl acrylate to allyl acrylate were also used to study the
interesterification reaction between dichloropropyl dodecanoate
and ethyl acrylate. Table 2 shows that all the tested biocatalysts
were able to catalyse to some extent this new interesterification
reaction. Although CALB was again the best biocatalysts among
those studied, yields were much lower than those obtained in the
Table 2
Percentage of dichloropropyl acrylate obtained using diverse commercial enzymes and resting cells with lipase activity. Reaction time 1 h.
Biocatalyst
Biocatalyst support
Temperature (◦C)
Yield (%)
Biocatalyst concentration (%w/w)a
3.3
15
CALB
PS-IM
Acrylic resin
50
50
50
40
50
40
40
40
7.0 0.3
6.2 0.2
6.7 0.1
5.1 0.4
5.4 0.7
3.4 0.5
5.5 0.6
6.0 0.2
10.4 0.2
7.8 0.3
9.7 0.2
5.2 0.3
5.6 0.2
4.7 0.1
5.6 0.8
6.6 0.7
Diatomaceous earth
Ion-exchange resin
Immobead 150
Powder, free enzyme
Resting cells
MmL 1
IM-150
PsL
R. oryzae (3)
A. fumigatus
A. flavus
Resting cells
Resting cells
a
Based on dichloropropyl dodecanoate weight.

E. Yara-Varón et al. / Catalysis Today 196 (2012) 86–90
89
O
O
O
O
R2
Biocatalyst
R2
+
+
R1
O
R1
O
O
O
R1= CH3(CH2)10
-
R2= -CH2CH=CH2 or -CH(CH2Cl)2
Scheme 1. General scheme of the biocatalytic production of allyl and dichloropropyl acrylates.
Once CALB was found as the best biocatalyst among those
studied to interesterificate ethyl acrylate, the possible effects of
a molar ratio of 1:5 between ethyl acrylate and wither allyl and
dichloropropyl dodecanoates were studied. When an excess of allyl
dodecanoate was used, the maximum yield of allyl acrylate was 29%
using 15% (w/w) biocatalyst, compared to 45% when an equimolar
ratio was used. The dichloropropyl acrylate yield also decreased
from 10.43% to 6.02%. Considering all of these results, a 1:1 ratio
of ethyl acrylate to allyl dodecanoate was used for all subsequent
experiments. Fig. 2 shows the influence of water activity in the allyl
acrylate conversion. The best conversion was observed using the
biocatalyst either as received (aw = 0.55) or after drying (aw = 0.33).
The biocatalyst with the highest aw tested (aw = 0.81) gave the worst
conversion. These results are in accordance with those described by
Petersson et al. for the synthesis of cetyl palmitate [36].
Fig. 2. Influence of water activity on the conversion of ethyl acrylate to allyl acrylate.
The reaction was carried out at 50 ◦C for 24 h using CALB at concentrations of 3.3%
(w/w) and 15% (w/w) based on the weight of allyl dodecanoate.
Finally, CALB was used to interesterificate two different alkyl
acrylates and acrylic acid. Table 3 shows that whereas butyl acrylate
gave similar yields as ethyl acrylate, ethyl methacrylate and acrylic
acid gave worse yields. Diverse authors have already described sim-
ilar results during transacylation studies using several alcohols and
CALB in various solvents [21,37,38]. Syrén and Hult [38] justified
the lower conversions found using methyl methacrylate consid-
ering the conformomers present in the transition state. According
Table 3
Influence of the alkyl acrylate reagent on conversion to the corresponding allyl
acrylic ester. The reaction was carried out at 50 ◦C for 1 h using CALB at 3.3% (w/w)
and 15% (w/w) based on the weight of allyl dodecanoate and aw = 0.55.
Reagents
Yield (%)
Biocatalyst concentration
(% w/w)
3.3
15
Butyl acrylate/allyl dodecanoate
Acrylic acid/allyl dodecanoate
Ethyl methacrylate/allyl dodecanoate
17.0 0.0
5.6 0.1
12.2 0.3
45.1 0.1
14.7 0.1
34.2 1.2
to these authors, only two of these possible conformomers of the
bond olefinic were able to be transacylated. They called these the
s-cis and s-trans conformations. They determined that 0.003 was
the relative probability of forming one of these productive con-
formomers for methyl methacrylate, whereas for methyl acrylate,
this probability increased up to 0.279. Using this approach, they
obtained a rationally designed CALB V190A mutant with higher
catalytic activity towards methyl methacrylate (Scheme 1).
4. Conclusions
A new biocatalytic interesterification reaction between acrylic
carboxylates and both allyl and dichloropropyl dodecanoates in a
solvent-free system has been described. The reaction allows the
preparation of allyl and dichloropropyl acrylates using diverse
commercial biocatalysts. The interesterification of dichloropropyl
dodecanoate always gave lower yields than using allyl dode-
canoate. Some resting cells with lipase-like activity could catalyse
the reaction, but always with low to moderate yields. The best bio-
catalyst among those studied was the commercial enzyme CALB.
The reaction using allyl dodecanoate was moisture sensitive, as we
observed a decrease in the conversion yield when the highest water
activity was used. CALB could be also applied to diverse acrylic
compounds, although the yield of allyl acrylates decreased using
Fig. 1. Influence of the biocatalyst on the conversion of ethyl acrylate to allyl acry-
late. The reaction was carried out at 50 ◦C for 24 h using three different biocatalysts.
(A) 3.3% (w/w) biocatalyst based on the weight of allyl dodecanoate. (B) 15% (w/w)
biocatalyst based on the weight of allyl dodecanoate.

90
E. Yara-Varón et al. / Catalysis Today 196 (2012) 86–90
both ethyl methacrylate and acrylic acid. Studies are underway to
prepare copolymers from the reaction mixtures obtained.
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