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Milena Corredig - One of the best experts on this subject based on the ideXlab platform.
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vitamin d3 and phytosterols affect the properties of Polyglycerol Polyricinoleate pgpr and protein interfaces
Food Hydrocolloids, 2016Co-Authors: Jonathan Andrade, Milena CorredigAbstract:Abstract The present work tested the effect of addition of hydrophobic compounds at interfaces containing Polyglycerol Polyricinoleate (PGPR) and β-lactoglobulin or sodium caseinate, using drop tensiometry. Vitamin D3 or phytosterols were also tested on a model double emulsion stabilized with PGPR and sodium caseinate. Emulsions were prepared using a high pressure homogenizer, and changes in particle size were followed using light scattering. The encapsulation efficiency of the double emulsions was estimated by adding Mg 2+ and measuring its release from the inner droplet. PGPR dominated the oil-water interfacial properties. In the presence of proteins there was a decrease of the interfacial tension, with little changes in the viscoelastic properties. The presence of vitamin D3 and phytosterols further affected the interfacial properties. Double emulsions were then prepared with 2% PGPR. While control emulsions showed limited stability with an increase in the particle size after one week of storage, emulsions containing 0.05% (w/w) of vitamin D3 or phytosterol resulted in better stability over the storage period. Results suggested that vitamin D 3 and phytosterol molecules may interact with the emulsifiers at the interface, affecting the physico-chemical properties, and possibly their release during digestion.
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The effect of calcium on the composition and physical properties of whey protein particles prepared using emulsification.
Food Chemistry, 2014Co-Authors: Nieke Westerik, Elke Scholten, Milena CorredigAbstract:Protein microparticles were formed through emulsification of 25% (w/w) whey protein isolate (WPI) solutions containing various concentrations of calcium (0.0–400.0 mM) in an oil phase stabilized by Polyglycerol Polyricinoleate (PGPR). The emulsions were heated (at 80 °C) and the microparticles subsequently re-dispersed in an aqueous phase. Light microscopy and scanning electron microscopy (SEM) images revealed that control particles and those prepared with 7.4 mM calcium were spherical and smooth. Particles prepared with 15.0 mM calcium gained an irregular, cauliflower-like structure, and at concentrations larger than 30.0 mM, shells formed and the particles were no longer spherical. These results describe, for the first time, the potential of modulating the properties of dense whey protein particles by using calcium, and may be used as structuring agents for the design of functional food matrices with increased protein and calcium content.
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interactions between Polyglycerol Polyricinoleate pgpr and pectins at the oil water interface and their influence on the stability of water in oil emulsions
Food Hydrocolloids, 2014Co-Authors: Ibrahim Gulseren, Milena CorredigAbstract:Abstract The interactions between a hydrophobic emulsifier (Polyglycerol Polyricinoleate) and pectin at the oil–water interface were studied using drop shape tensiometry, and the results were related to the emulsifying behavior of these ingredients in water-in-oil emulsions. High methoxyl pectin (HMP) and sugar beet pectin (SBP) were used as model polysaccharides, because of their differences in interfacial activity. Pectins were added to the aqueous phase in the absence and presence of PGPR in the oil phase. SBP was shown to further decrease the interfacial tension when added simultaneously with PGPR. In the presence of PGPR, SBP or HMP caused the formation of a weakly elastic interfacial film. Water-in-oil emulsions containing PGPR (2–6%) showed improved stability when containing SBP or HMP (0.1%), compared to water alone. This work highlights the potential for reducing the amount of PGPR added to water-in-oil emulsions by creating interacting films with polysaccharides at the oil–water interface.
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Interactions between Polyglycerol Polyricinoleate (PGPR) and pectins at the oil–water interface and their influence on the stability of water-in-oil emulsions
Food Hydrocolloids, 2012Co-Authors: Ibrahim Gulseren, Milena CorredigAbstract:Abstract The interactions between a hydrophobic emulsifier (Polyglycerol Polyricinoleate) and pectin at the oil–water interface were studied using drop shape tensiometry, and the results were related to the emulsifying behavior of these ingredients in water-in-oil emulsions. High methoxyl pectin (HMP) and sugar beet pectin (SBP) were used as model polysaccharides, because of their differences in interfacial activity. Pectins were added to the aqueous phase in the absence and presence of PGPR in the oil phase. SBP was shown to further decrease the interfacial tension when added simultaneously with PGPR. In the presence of PGPR, SBP or HMP caused the formation of a weakly elastic interfacial film. Water-in-oil emulsions containing PGPR (2–6%) showed improved stability when containing SBP or HMP (0.1%), compared to water alone. This work highlights the potential for reducing the amount of PGPR added to water-in-oil emulsions by creating interacting films with polysaccharides at the oil–water interface.
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interactions at the interface between hydrophobic and hydrophilic emulsifiers Polyglycerol Polyricinoleate pgpr and milk proteins studied by drop shape tensiometry
Food Hydrocolloids, 2012Co-Authors: Ibrahim Gulseren, Milena CorredigAbstract:Abstract The equilibrium interfacial tension and dilational elasticity at the soy oil–water interface were studied in the presence of a lipophilic emulsifier, Polyglycerol Polyricinoleate (PGPR), in the continuous oil phase, and dairy proteins, β-lactoglobulin (β-lg) or sodium caseinate, in the aqueous phase using drop shape tensiometry. The interfacial tension decreased with increasing PGPR concentration, and was
S. Ortega - One of the best experts on this subject based on the ideXlab platform.
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Solvent-free biocatalytic synthesis of Polyglycerol Polyricinoleate (PGPR) using immobilised Candida rugosa and Rhizopus arrhizus lipases
Lipase: Functions Synthesis and Role in Disease, 2012Co-Authors: S. Ortega, M F Maximo, M C Montiel, Jaume BastidaAbstract:The use of lipases is continuously increasing due to its ability to catalyse esterification, interesterification, acidolysis, alcoholysis and aminolysis in addition to the hydrolytic activity on triglycerides, to produce industrially important products such as emulsifiers, surfactants, wax esters, chiral molecules, biopolymers, modified fats and oils, structured lipids, and flavour esters.We have developed the biocatalytic synthesis of a food additive named Polyglycerol Polyricinoleate (PGPR) and identified with the code E-476.PGPR is widely known as an excellent water-in-oil emulsifier in the food industry, because it forms very stable emulsions even when the water content is very high, such as 80%. Therefore, PGPR is used as emulsifier in tin-greasing emulsions for the baking trade, and for the production of low-fat spreads. However, the main application of PGPR is in the chocolate industry, where is used in the adjustment of rheological properties of chocolate, improving the moulding properties of the molten chocolate. An additional property of PGPR in chocolate is its ability to limit fat bloom.The enzymatic synthesis of PGPR by the catalytic action of one or more lipases (which act in mild reaction conditions of temperature and pressure, neutral pH and in a solvent-free system), makes the process environmentally friendly and avoids side reactions so that the obtained product has a higher purity and quality than the current marketed PGPR obtained by chemical processes. © 2012 Nova Science Publishers, Inc. All rights reserved.
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solvent free Polyglycerol Polyricinoleate synthesis mediated by lipase from rhizopus arrhizus
Biochemical Engineering Journal, 2011Co-Authors: J.l. Gomez, M F Maximo, M C Montiel, M D Murcia, Jaume Bastida, S. OrtegaAbstract:Abstract The enzymatic biosynthesis of Polyglycerol Polyricinoleate (PGPR) (E-476) is described in detail for the first time. Starting from Polyglycerol and polyricinoleic acid, Rhizopus arrhizus lipase was used as catalyst. The reaction, which is really a reversal of hydrolysis, takes place in the presence of a very limited amount of aqueous phase. No organic solvent is necessary to solubilise the substrates, which allows a reaction medium solely composed of the necessary substrates to be used. Immobilisation of the lipase by physical adsorption onto an anion exchange resin provided good results in terms of activity, enzyme stability and the reuse of immobilised derivative. Using this immobilised derivative, PGPR with an acid value of 16 mg KOH/g was obtained, far above the requirements of the European Commission Directive 2008/84/EC (
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screening and selection of lipases for the enzymatic production of Polyglycerol Polyricinoleate
Biochemical Engineering Journal, 2009Co-Authors: A Bodalo, M F Maximo, M C Montiel, Jaume Bastida, M Gomez, S. OrtegaAbstract:We have demonstrated, for the first time, that Polyglycerol Polyricinoleate (PGPR) can be synthesized using lipases as biocatalyst with very good results. Of the twenty-one lipases screened for their ability to catalyse PGPR production from a mixture of polyricinoleic acid and Polyglycerol-3, only twelve lipases were able to catalyse the reaction. All of them were from microbial sources (bacteria and fungi) and were 1,3-specific or “random” lipases. The selection procedure was based not only on the enzymatic activity but also on economic criteria. Lipases from Mucor javanicus, Rhizopus arrhizus and Rhizopus oryzae were finally chosen, and all three enzymes were successfully immobilized by adsorption onto an anion exchange resin where they showed their suitability to catalyse the synthesis of PGPR. This represents a promising starting point for developing an industrial process for the green production of Polyglycerol Polyricinoleate.
Jaume Bastida - One of the best experts on this subject based on the ideXlab platform.
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Biocatalytic Synthesis of Polymeric Esters Used as Emulsifiers
Chemical and Biochemical Engineering Quarterly, 2019Co-Authors: Salvadora Ortega-requena, M F Maximo, M C Montiel, Jaume Bastida, Mar Serrano-arnaldos, M. D. Murcia AlmagroAbstract:Polyglycerol Polyricinoleate (PGPR) is a polymeric ester widely used as emulsifier in the food industry. In this work, PGPR biocatalytic synthesis was carried out in a onestep solvent-free enzymatic process using lipase CALB immobilized in Lewatit® Monoplus<br /> MP 64 by adsorption. The optimal immobilization conditions were determined: initial<br /> enzyme concentration of 13 mg of Lowry protein per mL phosphate buffer pH 7, and<br /> ricinoleic acid as a support activator. An immobilized derivative with 35.93 ± 4.90 mg of<br /> Lowry protein per g of dry support was obtained. It was used as a catalyst for PGPR<br /> production in open air and vacuum batch reactors, and the results obtained showed that<br /> only when the reaction equilibrium was shifted towards ester production by means of water removal, the PGPR produced fulfilled the European legislation (acid value ≤ 6 mg of KOH per g of product).
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study of different reaction schemes for the enzymatic synthesis of Polyglycerol Polyricinoleate
Journal of the Science of Food and Agriculture, 2014Co-Authors: Salvadora Ortegarequena, M C Montiel, J.l. Gomez, Jaume Bastida, Fuensanta Maximo, M D MurciaAbstract:BACKGROUND Different strategies for the solvent-free enzymatic production of Polyglycerol Polyricinoleate (PGPR) were explored in an attempt to simplify and improve the process. Besides the conventional procedure (obtaining polyricinoleic acid, followed by its esterification with Polyglycerol), two alternative methods are proposed: (1) reversing the synthesis order, i.e. esterification of Polyglycerol with ricinoleic acid and then the condensation of ricinoleic acid with the previously obtained Polyglycerol ester; and (2) the enzymatic synthesis of PGPR in a single-step process. RESULTS The reaction sequences were carried out in an open-air reactor with free and immobilised lipases (triacylglycerol acylhydrolases, E.C. 3.1.1.3): Candida rugosa lipase to obtain polyricinoleic acid and Rhizopus oryzae lipase for the esterification of Polyglycerol with the carboxyl group of ricinoleic or polyricinoleic acid. A co-immobilised derivative containing both lipases was used to catalyse the single-stage scheme. The three processes were carried out in a vacuum reactor, obtaining in every case PGPR that complied with the legal specifications of the European Community and recommendations provided in the Food Chemical Codex. CONCLUSION The results demonstrate that all three protocols are viable for the enzymatic synthesis of PGPR and require similar reaction times. The single-stage scheme is easier to carry out. © 2014 Society of Chemical Industry
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Solvent-free biocatalytic synthesis of Polyglycerol Polyricinoleate (PGPR) using immobilised Candida rugosa and Rhizopus arrhizus lipases
Lipase: Functions Synthesis and Role in Disease, 2012Co-Authors: S. Ortega, M F Maximo, M C Montiel, Jaume BastidaAbstract:The use of lipases is continuously increasing due to its ability to catalyse esterification, interesterification, acidolysis, alcoholysis and aminolysis in addition to the hydrolytic activity on triglycerides, to produce industrially important products such as emulsifiers, surfactants, wax esters, chiral molecules, biopolymers, modified fats and oils, structured lipids, and flavour esters.We have developed the biocatalytic synthesis of a food additive named Polyglycerol Polyricinoleate (PGPR) and identified with the code E-476.PGPR is widely known as an excellent water-in-oil emulsifier in the food industry, because it forms very stable emulsions even when the water content is very high, such as 80%. Therefore, PGPR is used as emulsifier in tin-greasing emulsions for the baking trade, and for the production of low-fat spreads. However, the main application of PGPR is in the chocolate industry, where is used in the adjustment of rheological properties of chocolate, improving the moulding properties of the molten chocolate. An additional property of PGPR in chocolate is its ability to limit fat bloom.The enzymatic synthesis of PGPR by the catalytic action of one or more lipases (which act in mild reaction conditions of temperature and pressure, neutral pH and in a solvent-free system), makes the process environmentally friendly and avoids side reactions so that the obtained product has a higher purity and quality than the current marketed PGPR obtained by chemical processes. © 2012 Nova Science Publishers, Inc. All rights reserved.
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solvent free Polyglycerol Polyricinoleate synthesis mediated by lipase from rhizopus arrhizus
Biochemical Engineering Journal, 2011Co-Authors: J.l. Gomez, M F Maximo, M C Montiel, M D Murcia, Jaume Bastida, S. OrtegaAbstract:Abstract The enzymatic biosynthesis of Polyglycerol Polyricinoleate (PGPR) (E-476) is described in detail for the first time. Starting from Polyglycerol and polyricinoleic acid, Rhizopus arrhizus lipase was used as catalyst. The reaction, which is really a reversal of hydrolysis, takes place in the presence of a very limited amount of aqueous phase. No organic solvent is necessary to solubilise the substrates, which allows a reaction medium solely composed of the necessary substrates to be used. Immobilisation of the lipase by physical adsorption onto an anion exchange resin provided good results in terms of activity, enzyme stability and the reuse of immobilised derivative. Using this immobilised derivative, PGPR with an acid value of 16 mg KOH/g was obtained, far above the requirements of the European Commission Directive 2008/84/EC (
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screening and selection of lipases for the enzymatic production of Polyglycerol Polyricinoleate
Biochemical Engineering Journal, 2009Co-Authors: A Bodalo, M F Maximo, M C Montiel, Jaume Bastida, M Gomez, S. OrtegaAbstract:We have demonstrated, for the first time, that Polyglycerol Polyricinoleate (PGPR) can be synthesized using lipases as biocatalyst with very good results. Of the twenty-one lipases screened for their ability to catalyse PGPR production from a mixture of polyricinoleic acid and Polyglycerol-3, only twelve lipases were able to catalyse the reaction. All of them were from microbial sources (bacteria and fungi) and were 1,3-specific or “random” lipases. The selection procedure was based not only on the enzymatic activity but also on economic criteria. Lipases from Mucor javanicus, Rhizopus arrhizus and Rhizopus oryzae were finally chosen, and all three enzymes were successfully immobilized by adsorption onto an anion exchange resin where they showed their suitability to catalyse the synthesis of PGPR. This represents a promising starting point for developing an industrial process for the green production of Polyglycerol Polyricinoleate.
M C Montiel - One of the best experts on this subject based on the ideXlab platform.
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Biocatalytic Synthesis of Polymeric Esters Used as Emulsifiers
Chemical and Biochemical Engineering Quarterly, 2019Co-Authors: Salvadora Ortega-requena, M F Maximo, M C Montiel, Jaume Bastida, Mar Serrano-arnaldos, M. D. Murcia AlmagroAbstract:Polyglycerol Polyricinoleate (PGPR) is a polymeric ester widely used as emulsifier in the food industry. In this work, PGPR biocatalytic synthesis was carried out in a onestep solvent-free enzymatic process using lipase CALB immobilized in Lewatit® Monoplus<br /> MP 64 by adsorption. The optimal immobilization conditions were determined: initial<br /> enzyme concentration of 13 mg of Lowry protein per mL phosphate buffer pH 7, and<br /> ricinoleic acid as a support activator. An immobilized derivative with 35.93 ± 4.90 mg of<br /> Lowry protein per g of dry support was obtained. It was used as a catalyst for PGPR<br /> production in open air and vacuum batch reactors, and the results obtained showed that<br /> only when the reaction equilibrium was shifted towards ester production by means of water removal, the PGPR produced fulfilled the European legislation (acid value ≤ 6 mg of KOH per g of product).
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study of different reaction schemes for the enzymatic synthesis of Polyglycerol Polyricinoleate
Journal of the Science of Food and Agriculture, 2014Co-Authors: Salvadora Ortegarequena, M C Montiel, J.l. Gomez, Jaume Bastida, Fuensanta Maximo, M D MurciaAbstract:BACKGROUND Different strategies for the solvent-free enzymatic production of Polyglycerol Polyricinoleate (PGPR) were explored in an attempt to simplify and improve the process. Besides the conventional procedure (obtaining polyricinoleic acid, followed by its esterification with Polyglycerol), two alternative methods are proposed: (1) reversing the synthesis order, i.e. esterification of Polyglycerol with ricinoleic acid and then the condensation of ricinoleic acid with the previously obtained Polyglycerol ester; and (2) the enzymatic synthesis of PGPR in a single-step process. RESULTS The reaction sequences were carried out in an open-air reactor with free and immobilised lipases (triacylglycerol acylhydrolases, E.C. 3.1.1.3): Candida rugosa lipase to obtain polyricinoleic acid and Rhizopus oryzae lipase for the esterification of Polyglycerol with the carboxyl group of ricinoleic or polyricinoleic acid. A co-immobilised derivative containing both lipases was used to catalyse the single-stage scheme. The three processes were carried out in a vacuum reactor, obtaining in every case PGPR that complied with the legal specifications of the European Community and recommendations provided in the Food Chemical Codex. CONCLUSION The results demonstrate that all three protocols are viable for the enzymatic synthesis of PGPR and require similar reaction times. The single-stage scheme is easier to carry out. © 2014 Society of Chemical Industry
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Solvent-free biocatalytic synthesis of Polyglycerol Polyricinoleate (PGPR) using immobilised Candida rugosa and Rhizopus arrhizus lipases
Lipase: Functions Synthesis and Role in Disease, 2012Co-Authors: S. Ortega, M F Maximo, M C Montiel, Jaume BastidaAbstract:The use of lipases is continuously increasing due to its ability to catalyse esterification, interesterification, acidolysis, alcoholysis and aminolysis in addition to the hydrolytic activity on triglycerides, to produce industrially important products such as emulsifiers, surfactants, wax esters, chiral molecules, biopolymers, modified fats and oils, structured lipids, and flavour esters.We have developed the biocatalytic synthesis of a food additive named Polyglycerol Polyricinoleate (PGPR) and identified with the code E-476.PGPR is widely known as an excellent water-in-oil emulsifier in the food industry, because it forms very stable emulsions even when the water content is very high, such as 80%. Therefore, PGPR is used as emulsifier in tin-greasing emulsions for the baking trade, and for the production of low-fat spreads. However, the main application of PGPR is in the chocolate industry, where is used in the adjustment of rheological properties of chocolate, improving the moulding properties of the molten chocolate. An additional property of PGPR in chocolate is its ability to limit fat bloom.The enzymatic synthesis of PGPR by the catalytic action of one or more lipases (which act in mild reaction conditions of temperature and pressure, neutral pH and in a solvent-free system), makes the process environmentally friendly and avoids side reactions so that the obtained product has a higher purity and quality than the current marketed PGPR obtained by chemical processes. © 2012 Nova Science Publishers, Inc. All rights reserved.
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solvent free Polyglycerol Polyricinoleate synthesis mediated by lipase from rhizopus arrhizus
Biochemical Engineering Journal, 2011Co-Authors: J.l. Gomez, M F Maximo, M C Montiel, M D Murcia, Jaume Bastida, S. OrtegaAbstract:Abstract The enzymatic biosynthesis of Polyglycerol Polyricinoleate (PGPR) (E-476) is described in detail for the first time. Starting from Polyglycerol and polyricinoleic acid, Rhizopus arrhizus lipase was used as catalyst. The reaction, which is really a reversal of hydrolysis, takes place in the presence of a very limited amount of aqueous phase. No organic solvent is necessary to solubilise the substrates, which allows a reaction medium solely composed of the necessary substrates to be used. Immobilisation of the lipase by physical adsorption onto an anion exchange resin provided good results in terms of activity, enzyme stability and the reuse of immobilised derivative. Using this immobilised derivative, PGPR with an acid value of 16 mg KOH/g was obtained, far above the requirements of the European Commission Directive 2008/84/EC (
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screening and selection of lipases for the enzymatic production of Polyglycerol Polyricinoleate
Biochemical Engineering Journal, 2009Co-Authors: A Bodalo, M F Maximo, M C Montiel, Jaume Bastida, M Gomez, S. OrtegaAbstract:We have demonstrated, for the first time, that Polyglycerol Polyricinoleate (PGPR) can be synthesized using lipases as biocatalyst with very good results. Of the twenty-one lipases screened for their ability to catalyse PGPR production from a mixture of polyricinoleic acid and Polyglycerol-3, only twelve lipases were able to catalyse the reaction. All of them were from microbial sources (bacteria and fungi) and were 1,3-specific or “random” lipases. The selection procedure was based not only on the enzymatic activity but also on economic criteria. Lipases from Mucor javanicus, Rhizopus arrhizus and Rhizopus oryzae were finally chosen, and all three enzymes were successfully immobilized by adsorption onto an anion exchange resin where they showed their suitability to catalyse the synthesis of PGPR. This represents a promising starting point for developing an industrial process for the green production of Polyglycerol Polyricinoleate.
M F Maximo - One of the best experts on this subject based on the ideXlab platform.
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Biocatalytic Synthesis of Polymeric Esters Used as Emulsifiers
Chemical and Biochemical Engineering Quarterly, 2019Co-Authors: Salvadora Ortega-requena, M F Maximo, M C Montiel, Jaume Bastida, Mar Serrano-arnaldos, M. D. Murcia AlmagroAbstract:Polyglycerol Polyricinoleate (PGPR) is a polymeric ester widely used as emulsifier in the food industry. In this work, PGPR biocatalytic synthesis was carried out in a onestep solvent-free enzymatic process using lipase CALB immobilized in Lewatit® Monoplus<br /> MP 64 by adsorption. The optimal immobilization conditions were determined: initial<br /> enzyme concentration of 13 mg of Lowry protein per mL phosphate buffer pH 7, and<br /> ricinoleic acid as a support activator. An immobilized derivative with 35.93 ± 4.90 mg of<br /> Lowry protein per g of dry support was obtained. It was used as a catalyst for PGPR<br /> production in open air and vacuum batch reactors, and the results obtained showed that<br /> only when the reaction equilibrium was shifted towards ester production by means of water removal, the PGPR produced fulfilled the European legislation (acid value ≤ 6 mg of KOH per g of product).
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Solvent-free biocatalytic synthesis of Polyglycerol Polyricinoleate (PGPR) using immobilised Candida rugosa and Rhizopus arrhizus lipases
Lipase: Functions Synthesis and Role in Disease, 2012Co-Authors: S. Ortega, M F Maximo, M C Montiel, Jaume BastidaAbstract:The use of lipases is continuously increasing due to its ability to catalyse esterification, interesterification, acidolysis, alcoholysis and aminolysis in addition to the hydrolytic activity on triglycerides, to produce industrially important products such as emulsifiers, surfactants, wax esters, chiral molecules, biopolymers, modified fats and oils, structured lipids, and flavour esters.We have developed the biocatalytic synthesis of a food additive named Polyglycerol Polyricinoleate (PGPR) and identified with the code E-476.PGPR is widely known as an excellent water-in-oil emulsifier in the food industry, because it forms very stable emulsions even when the water content is very high, such as 80%. Therefore, PGPR is used as emulsifier in tin-greasing emulsions for the baking trade, and for the production of low-fat spreads. However, the main application of PGPR is in the chocolate industry, where is used in the adjustment of rheological properties of chocolate, improving the moulding properties of the molten chocolate. An additional property of PGPR in chocolate is its ability to limit fat bloom.The enzymatic synthesis of PGPR by the catalytic action of one or more lipases (which act in mild reaction conditions of temperature and pressure, neutral pH and in a solvent-free system), makes the process environmentally friendly and avoids side reactions so that the obtained product has a higher purity and quality than the current marketed PGPR obtained by chemical processes. © 2012 Nova Science Publishers, Inc. All rights reserved.
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solvent free Polyglycerol Polyricinoleate synthesis mediated by lipase from rhizopus arrhizus
Biochemical Engineering Journal, 2011Co-Authors: J.l. Gomez, M F Maximo, M C Montiel, M D Murcia, Jaume Bastida, S. OrtegaAbstract:Abstract The enzymatic biosynthesis of Polyglycerol Polyricinoleate (PGPR) (E-476) is described in detail for the first time. Starting from Polyglycerol and polyricinoleic acid, Rhizopus arrhizus lipase was used as catalyst. The reaction, which is really a reversal of hydrolysis, takes place in the presence of a very limited amount of aqueous phase. No organic solvent is necessary to solubilise the substrates, which allows a reaction medium solely composed of the necessary substrates to be used. Immobilisation of the lipase by physical adsorption onto an anion exchange resin provided good results in terms of activity, enzyme stability and the reuse of immobilised derivative. Using this immobilised derivative, PGPR with an acid value of 16 mg KOH/g was obtained, far above the requirements of the European Commission Directive 2008/84/EC (
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screening and selection of lipases for the enzymatic production of Polyglycerol Polyricinoleate
Biochemical Engineering Journal, 2009Co-Authors: A Bodalo, M F Maximo, M C Montiel, Jaume Bastida, M Gomez, S. OrtegaAbstract:We have demonstrated, for the first time, that Polyglycerol Polyricinoleate (PGPR) can be synthesized using lipases as biocatalyst with very good results. Of the twenty-one lipases screened for their ability to catalyse PGPR production from a mixture of polyricinoleic acid and Polyglycerol-3, only twelve lipases were able to catalyse the reaction. All of them were from microbial sources (bacteria and fungi) and were 1,3-specific or “random” lipases. The selection procedure was based not only on the enzymatic activity but also on economic criteria. Lipases from Mucor javanicus, Rhizopus arrhizus and Rhizopus oryzae were finally chosen, and all three enzymes were successfully immobilized by adsorption onto an anion exchange resin where they showed their suitability to catalyse the synthesis of PGPR. This represents a promising starting point for developing an industrial process for the green production of Polyglycerol Polyricinoleate.