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. 2018 Jun 21;19(7):1829.
doi: 10.3390/ijms19071829.

Lipase Immobilization on Silica Xerogel Treated with Protic Ionic Liquid and its Application in Biodiesel Production from Different Oils

Nayára B Carvalho  1   2 , Bruna T Vidal  3 , Anderson S Barbosa  4 , Matheus M Pereira  5 , Silvana Mattedi  6 , Lisiane Dos S Freitas  7 , Álvaro S Lima  8   9 , Cleide M F Soares  10   11
Affiliations

Lipase Immobilization on Silica Xerogel Treated with Protic Ionic Liquid and its Application in Biodiesel Production from Different Oils

Nayára B Carvalho et al. Int J Mol Sci. .

Abstract

Treated silica xerogel with protic ionic liquid (PIL) and bifunctional agents (glutaraldehyde and epichlorohydrin) is a novel support strategy used in the effective immobilization of lipase from Burkholderia cepacia (LBC) by covalent binding. As biocatalysts with the highest activity recovery yields, LBC immobilized by covalent binding with epichlorohydrin without (203%) and with PIL (250%), was assessed by the following the hydrolysis reaction of olive oil and characterized biochemically (Michaelis⁻Menten constant, optimum pH and temperature, and operational stability). Further, the potential transesterification activity for three substrates: sunflower, soybean, and colza oils, was also determined, achieving a conversion of ethyl esters between 70 and 98%. The supports and the immobilized lipase systems were characterized using Fourier transform infrared spectra (FTIR), scanning electron microscopy (SEM), elemental analysis, and thermogravimetric (TG) analysis.

Keywords: hydrolysis; immobilization; lipase; protic ionic liquid; transesterification; treated silica xerogel support.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Effects on relative activity under various pH and temperature values. Ranging from pH 2 to pH 10 at 37 °C for lipase from Burkholderia cepacia free (LBC) (■), lipase immobilized by covalent binding with epichlorohydrin onto support produced without ionic liquid (CBE-SC) (●), lipase immobilized by covalent binding with epichlorohydrin onto support produced with IL (CBE-SIL) (▲).
Figure 2
Figure 2
Effects on relative activity under ranging from 25 to 80 °C for lipase from Burkholderia cepacia free (LBC), pH 7.0 (■), lipase immobilized by covalent binding with epichlorohydrin onto support produced without IL (CBE-SC), pH 3.0 (●), lipase immobilized by covalent binding with epichlorohydrin onto support produced with IL a(CBE-SIL), pH 3.0 (▲).
Figure 3
Figure 3
Operational stability of the lipase from Burkholderia cepacia immobilized by covalent binding. Reactional conditions were: 45 °C, pH 3.0, during 10 min and 80 rpm.
Figure 4
Figure 4
Scanning electron micrographs of SC (a); SIL indicating the black arrows a more porous and irregular surface (b) and CBE-SC (c) and CBE-SIL (d) indicating the black arrows possibly the presence of lipase due to its characteristic rounded shape.
Figure 5
Figure 5
FTIR spectra of the lipase from Burkholderia cepacia (LBC free), control silica (SC), silica produced with protic ionic liquid (SIL), lipase immobilized by covalent binding with epichlorohydrin onto silica control (CBE-SC) or lipase immobilized by covalent binding with epichlorohydrin onto silica produced with protic ionic liquid (CBE-SIL).
Figure 6
Figure 6
Time course of ethyl ester conversion using lipase from Burkholderia cepacia immobilized by covalent binding for different oils: soybean (a), sunflower (b) or colza (c). Experiments considered under a 40 °C, 96 h of reaction and stirring at 80 rpm. In image (d) a comparison between the three oil types for aliquots taken at 72 h of reaction under the already described conditions, is seen.
Scheme 1
Scheme 1
Possible reaction mechanisms of the silica support with functional activating agents glutaraldehyde and lipase.
Scheme 2
Scheme 2
Possible mechanism reactions for silica support with functional activating agents epichlorohydrin and lipase.
See this image and copyright information in PMC

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