Full Papers
doi.org/10.1002/cctc.202101050
ChemCatChem
Chemically Modified Lipase from Thermomyces lanuginosus
with Enhanced Esterification and Transesterification
Activities
Jennifer Noro,[a] Artur Cavaco-Paulo,*[a] and Carla Silva*[a]
Lipase from Thermomyces lanuginosus is one of the most
explored enzymes for the esterification of several added-value
industrial compounds, such as biodiesel, fragrances, and flavors.
Its selectivity in these reactions is mostly related with its activity
towards small alcohols. In this work, the impact of the chemical
modification, with 4 dodecyl chains at its surface, was evaluated
regarding its transesterification and esterification activities,
comparing with the native form. Linear size-differentiated
alcohols (from 1 to 20 carbons in the aliphatic chain) were used
to explore for the first time the effect of the chain length in
both transesterification and esterification reactions, using p-
nitrophenyl palmitate and oleic acid as model compounds,
respectively. The chemically modified lipase showed an out-
standing improvement of its catalytic performance than the
native enzyme, being this increase directly proportional to the
size of the alcohols chain used as substrates. The enormous
potential and remarkable versatility of this novel super catalyst
was here demonstrated, where diverse types of esters, differing
in their potential applications (biodiesel, cosmetics, fine
chemistry), were efficiently synthesized. The produced esters
were fully characterized by 1H NMR, GC-MS, and FTIR.
Introduction
stearic acid, being the produced esters isolated in good yields
(>60%).[7]
Lipase from Thermomyces lanuginosus (TL) was the first
recombinant lipase produced,[1] and nowadays, it remains one
of the most explored enzymes for the synthesis of compounds
with industrial value. Besides their natural triacylglycerols
hydrolysis function, it also demonstrates esterification and
transesterification activity.[2] Ester compounds are present in
many daily products, being the major components of flavors,
fragrances, polymers, fats, among others.[3] The use of lipases
for their synthesis is considered a green and environmentally
friendly practice, regarding the high reactional yields and the
mild reaction conditions associated.[4]
Among the different lipases, lipase TL is one of the most
explored for transesterification and esterification reactions.
Ashrafuzzaman and co-workers observed that immobilized
lipase TL demonstrated the highest regioselectivity in the
acylation of sucrose esters comparing to other lipases.[5] The
transesterification reaction was carried out using divinyl esters.
A similar approach was undertaken by Chávez-Flores et al.,[6] in
the regioselective transesterification of vinyl laurate with a
probiotic sugar, lactulose, using the same form of enzyme.
Corrêa and co-workers[7] studied the esterification of the flavors,
geraniol and citronellol, promoted by immobilized lipase TL.
The reactions were carried out by coupling oleic, lauric, and
The esterification of oleic acid with isoamyl alcohol was
performed by Lage et al..[8] The authors used lipase TL
immobilized onto polymethacrylate particles as reaction cata-
lyst. The ester, isoamyl oleate, which can be used as a
biolubricant, was successfully synthesized with high conversion
(85%).
Another major field of application of this lipase is in the
production of biodiesel. The extensive investigation reported in
this area stems from the world demand to find green and
renewable sources of fuels.[9] Biodiesel can be manufactured
through enzymatic catalysis, by the transesterification or
esterification of oils/fats with small-length alcohols, such as
methanol or ethanol. Countless sources of oils/fats can be used
for this purpose. Sunflower, coconut, soybean, palm, and cotton
seed oils or even wastes from the food industry, with varied
composition, are some of the potential sources.[10]
As described previously, most reports regarding transester-
ification and esterification reactions describe the use of lipase
TL in its immobilized form. The immobilization of enzymes
presents several advantages, in comparison to other method-
ologies, including reusability, thermostability, and others.[11]
However, immobilization techniques, besides being a more
expensive strategy, it reduces the enzyme mobility and
consequently, its catalytic performance.[12] Many reports form
literature have been describing the chemical modification of
lipases as an efficient methodology to overcome the limitations
associated to the immobilization methodologies.[13] However, a
lack of practical examples regarding its implementation on the
synthesis of industrial added-value products can be found. We
have previously reported that the PEGylation of lipase TL
improved its polymerase activity comparing with the native
[a] Dr. J. Noro, Prof. A. Cavaco-Paulo, Dr. C. Silva
Department of Biological Engineering
University of Minho
Campus de Gualtar
4710-057, Braga (Portugal)
E-mail: artur@deb.uminho.pt
ChemCatChem 2021, 13, 1–9
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