Sustainable preparation of a novel glycerol-free biofuel by using pig pancreatic lipase: Partial 1,3-regiospecific alcoholysis of sunflower oil

Caballero, Verónica; Bautista, Felipa M.; Campelo, J.M.; Luna, Diego; Marinas, J. M.; Romero, Antonio A.; Hidalgo, José Manuel Soto; Luque, Rafael; Macario, Anastasia; Giordano, G.

doi:10.1016/j.procbio.2008.11.015

Cited by 80 publications

(82 citation statements)

References 79 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…7 to 13) in which there is not enough ethanol to produce a complete transesterification, because only a 1:2 molar ratio of the reagents is not enough to complete the process. TOF values clearly indicate that an excess of ethanol, not only fails to give a 100% yield (which would lead to a standard biodiesel), but the transformation is even slower, similar to detected with the free enzymes [37]. Table 2 indicates that, with independence of the quality of raw materials, even using waste cooking oil and 96% ethanol, when employed a 1:3 molar ratio of oil/ethanol, similar TOF values are obtained independent of the oil/PPL ratio applied in the processes.…”

Section: Resultsmentioning

confidence: 65%

“…Enzymatic activities of immobilized PPL on amorphous AlPO 4 , an inorganic support, were determined as compared to free one, under different working conditions such as reaction temperature, reaction pH, oil/alcohol ratio and enzyme concentration. The effect of these different parameters in the preparation of biofuels by ethanolysis of sunflower oil was investigated in previous works using free PPL in order to optimise the reaction conditions [37][38][39]. Tables 1 and 2 summarise the results obtained employing the immobilized PPL compared to the free enzyme, in the transesterification reaction with a unique biocatalyst, constituted by immobilized PPL on AlPO 4.…”

Section: Resultsmentioning

confidence: 99%

“…Here, we report the application of an enzymatic protocol using free and covalent immobilized pig pancreatic lipase (PPL) to produce the 1,3-selective alcoholysis of sunflower oil with ethanol and other short chain alcohols. In this respect, in contrast to most studied lipases, the role played by the presence of minor amounts of NaOH water solutions in the activity improvement of the enzymatic process was noticeable in our reported methodology using PPL [37][38][39]. PPL is an extracellular lipase which actually operates in the digestive tract of mammalians under the higher pH values.…”

Section: Introductionmentioning

confidence: 93%

“…In the present case, it is not necessary to appeal to any especial ester because MGs are obtained by a partial alcoholysis of triglycerides (Scheme 1). This selective process was obtained via 1,3-regiospecific enzymatic alcoholysis of sunflower oil using some 1,3-regiospecific low cost lipase, like pig pancreatic lipase, PPL [37][38][39] or from Thermomyces lanuginosus (Lipopan 50 BG from Novozymes, Bagsvaerd, Denmark) [40]. Scheme 1.…”

Section: Introductionmentioning

confidence: 99%

“…As in the two methods described before [20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36], the already patented Ecodiesel-100 [37][38][39] obtained through the 1,3-selective partial ethanolysis of the triglycerides with PPL, is a mixture of two parts of FAEE and one part of MG, that integrates the glycerol as a soluble derivative product (MG) in the diesel fuel, but unlike these methods, no specific reagent (such as dimethyl carbonate or methyl acetate) more expensive than methanol (or ethanol) are used. This strategy is based on obtaining an incomplete alcoholysis by application of 1,3-selective lipases, so that the glycerol remains in the form of monoglyceride which avoids the production of glycerol as a by-product, reducing the environmental impact of the process.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Biofuel that Keeps Glycerol as Monoglyceride by 1,3-Selective Ethanolysis with Pig Pancreatic Lipase Covalently Immobilized on AlPO4 Support

et al. 2013

Self Cite

View full text Add to dashboard Cite

By using pig pancreatic lipase (EC 3.1.1.3 or PPL) as a biocatalyst, covalently immobilized on amorphous AlPO 4 support, a new second generation biodiesel was obtained in the transesterification reaction of sunflower oil with ethanol. The resulting biofuel is composed of fatty acid ethyl esters and monoglycerides (FAEE/MG) blended in a 2:1 molar ratio. This novel product, which integrates glycerol as monoacylglycerols (MG) into the biofuels composition, has similar physicochemical properties as conventional biodiesel and also avoids the removal step of the by-product by washing of the biodiesel with water. Immobilization of PPL was achieved by covalent attachment of the ε-amino group of the lysine residues of PPL with the aldehyde groups of p-hydroxybenzaldehyde linked on a hybrid organic-inorganic functionalized AlPO 4 surface. With this procedure, the PPL biocatalyst was strongly fixed to the inorganic support surface (94.3%). Nevertheless, the efficiency of the immobilized enzyme was relatively lower compared to that of the free PPL, but it showed a remarkable stability as well as a great capacity of reutilization (25 reuses) without a significant loss of its initial OPEN ACCESSEnergies 2013, 6 3880 catalytic activity. Therefore, this enzymatic method allows the production of a biodiesel which integrates the glycerol, allows a more efficient fabrication method and minimizes the waste production as compared to the conventional alkali-catalyzed process.

show abstract

Section: Resultsmentioning

confidence: 65%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Biofuel that Keeps Glycerol as Monoglyceride by 1,3-Selective Ethanolysis with Pig Pancreatic Lipase Covalently Immobilized on AlPO4 Support

et al. 2013

Self Cite

View full text Add to dashboard Cite

show abstract

Effects of methanol on lipases: Molecular, kinetic and process issues in the production of biodiesel

Lotti

Pleiss

Valero

et al. 2014

Biotechnology Journal

155

View full text Add to dashboard Cite

The biotechnological production of biodiesel is based on transesterification/esterification reactions between a source of fatty acids and a short-chain alcohol, usually methanol, catalysed by enzymes belonging to the class known as lipases. Several lipases used in industrial processes, although stable in the presence of other organic solvents, are inactivated by methanol at or below the concentration optimal for biodiesel production, making it necessary to use stepwise methanol feeding or pre-treatment of the enzyme. In this review article we focus on what is currently know about methanol inactivation of lipases, a phenomenon which is not common to all lipase enzymes, with the goal of improving the biocatalytic process. We suggest that different mechanisms can lead to inactivation of different lipases, in particular substrate inhibition and protein unfolding. Attempts to improve the performances of methanol sensitive lipases by mutagenesis as well as process engineering approaches are also summarized.

show abstract

1,3‐Regiospecific ethanolysis of soybean oil catalyzed by crosslinked porcine pancreas lipase aggregates

Ramos

Miranda

Giordano

et al. 2018

Biotechnology Progress

View full text Add to dashboard Cite

The preparation of crosslinked aggregates of pancreatic porcine lipase (PPL-CLEA) was systematically studied, evaluating the influence of three precipitants and two crosslinking agents, as well as the use of soy protein as an alternative feeder protein on the catalytic properties and stability of the immobilized PPL. Standard CLEAs showed a global yield (CLEA' observed activity/offered total activity) of less than 4%, whereas with the addition of soy protein (PPL:soy protein mass ratio of 1:3) the global yield was approximately fivefold higher. The CLEA of PPL prepared with soy protein as feeder (PPL:soy protein mass ratio of 1:3) and glutaraldehyde as crosslinking reagent (10 μmol of aldehyde groups/mg of total protein) was more active mainly because of the reduced enzyme leaching in the washing step. This CLEA, named PPL-SOY-CLEA, had an immobilization yield around 60% and an expressed activity around 40%. In the ethanolysis of soybean oil, the PPL-SOY-CLEA yielded maximum fatty acid ethyl ester (FAEE) concentration around 12-fold higher than that achieved using soluble PPL (34 h reaction at 30°C, 300 rpm stirring, soybean oil/ethanol molar ratio of 1:5) with an enzyme load around 2-fold lower (very likely due to free enzyme inactivation). The operational stability of the PPL-SOY-CLEA in the ethanolysis of soybean oil in a vortex flow type reactor showed that FAEE yield was higher than 50% during ten reaction cycles of 24 h. This reactor configuration may be an attractive alternative to the conventional stirred reactors for biotransformations in industrial plants using carrier-free biocatalysts. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:910-920, 2018.

show abstract

Sustainable preparation of a novel glycerol-free biofuel by using pig pancreatic lipase: Partial 1,3-regiospecific alcoholysis of sunflower oil

Cited by 80 publications

References 79 publications

Biofuel that Keeps Glycerol as Monoglyceride by 1,3-Selective Ethanolysis with Pig Pancreatic Lipase Covalently Immobilized on AlPO4 Support

Biofuel that Keeps Glycerol as Monoglyceride by 1,3-Selective Ethanolysis with Pig Pancreatic Lipase Covalently Immobilized on AlPO4 Support

Effects of methanol on lipases: Molecular, kinetic and process issues in the production of biodiesel

1,3‐Regiospecific ethanolysis of soybean oil catalyzed by crosslinked porcine pancreas lipase aggregates

Contact Info

Product

Resources

About