Browsing by Subject "Polyglycerol polyricinoleate"

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    Biocatalytic Synthesis of Polyglycerol Polyricinoleate: A Comparison of Different Commercial Lipases
    (Assoc. of Chemists and Chemical Engineers of Croatia, 2013-10) Ortega Requena, Salvadora; Gómez, José Luis; Bastida Rodríguez, Josefa; Máximo Martín, María Fuensanta; Montiel Morte, María Claudia; Gómez, María; Ingeniería Química
    In this work, the studies were carried out to select the most suitable lipase as catalyst for the esterification of polyglycerol with polyricinoleic acid to yield polyglicerol polyricinoleate (PGPR), a valued-added, biobased food emulsifier are described. The enzymes assayed were lipases from Rhizopus arrhizus, Rhizopus oryzae and Mucor javanicus, previously selected because of their suitable activity and moderate cost. First, reaction was catalyzed by free lipases in a batch reactor and the influence of different operating conditions (initial water content, amount of enzyme and temperature) on the progress of the reaction was studied. Next, the three lipases were immobilized by physical adsorption on the anion exchange resin, Lewatit MonoPlus MP 64, providing derivatives with a high activity and stability. Recovery of the immobilized derivative from the reaction medium was conducted with very good yields (up 99%) and no loss of activity of the derivative with successive uses was proved. Finally, a high performance reactor, which operates at low pressure and with a dry atmosphere, was used to synthesise PGPR using the immobilized enzymes. Both Rhizopus arrhizus and Rhizopus oryzae lipases allowed the production of a PGPR which fulfils the “specific purity criteria on food additives other than colours and sweeteners” established by the Commission of the European Communities, with an acid value of 4.91 and 5.31 mg KOH/g respectively.
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    Modification of oligo-Ricinoleic Acid and its derivatives with 10-undecenoic acid via lipase-catalyzed esterification
    (MDPI, 2012-04-17) Hayes, Douglas G.; Mannam, Vinay K.; Ye, Ran; Zhao, Haizhen; Ortega Requena, Salvadora; Montiel Morte, María Claudia; Ingeniería Química; Facultad de Química
    Lipases were employed under solvent-free conditions to conjugate oligo-ricinoleic acid derivatives with 10-undecenoic acid, to incorporate a reactive terminal double bond into the resultant product. First, undecenoic acid was covalently attached to oligo-ricinoleic acid using immobilized Candida antarctica lipase (CAL) at a 30% yield. Thirty percent conversion also occurred for CAL-catalyzed esterification between undecenoic acid and biocatalytically-prepared polyglycerol polyricinoleate (PGPR), with attachment of undecenoic acid occurring primarily at free hydroxyls of the polyglycerol moiety. The synthesis of oligo-ricinoleyl-, undecenoyl- structured triacylglycerols comprised two steps. The first step, the 1,3-selective lipase-catalyzed interesterification of castor oil with undecenoic acid, occurred successfully. The second step, the CAL-catalyzed reaction between ricinoleyl-, undecenoyl structured TAG and ricinoleic acid, yielded approximately 10% of the desired structured triacylglycerols (TAG); however, a significant portion of the ricinoleic acid underwent self-polymerization as a side-reaction. The employment of gel permeation chromatography, normal phase HPLC, NMR, and acid value measurements was effective for characterizing the reaction pathways and products that formed.
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    Optimized enzymatic synthesis of the food additive polyglycerol polyricinoleate (PGPR) using Novozym® 435 in a solvent free system
    (Elsevier, 2014-01-21) Ortega Requena, Salvadora; Bódalo-Santoyo, A.; Bastida Rodríguez, Josefa; Máximo, María Fuensanta; Montiel Morte, María Claudia; Gómez Gómez, María; Ingeniería Química; Facultad de Química
    Polyglycerol polyricinoleate (PGPR) is used as an emulsifier in the food industry, especially in chocolate coatings and chocolate bars. PGPR improves the characteristics of molten chocolate by reducing yield stress, facilitating the coating of confectionery pieces, while limiting the amount of cocoa butter involved. The enzymatic synthesis of PGPR catalyzed by lipases presents several advantages over chemical synthesis, including enzyme specificity and the mild conditions needed, thereby avoiding undesirable side-reactions and by-products. A novel process to synthesize PGPR using a biocatalyst, Novozym® 435, is presented. Novozym® 435 is appropriate for catalyzing both the reactions involved in this process. A PGPR fulfilling European specifications for this food additive as well as recommendations set out in the Food Chemical Codex, was obtained using a discontinuous vacuum reactor with a dry nitrogen flow. In addition, the biocatalyst reuse would decrease costs. Moreover, it was confirmed that the ability to obtain PGPR in a one-step reaction significantly shortens the time required.
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    SCREENING AND SELECTION OF LIPASES FOR THE ENZYMATIC PRODUCTION OF POLYGLYCEROL POLYRICINOLEATE
    (2009-05-07) Bódalo, A.; Bastida Rodríguez, Josefa; Máximo Martín, María Fuensanta; Montiel Morte, María Claudia; Gómez, M.; Ortega Requena, Salvadora; Ingeniería Química
    We have demonstrated, for the first time, that polyglylcerol polyricinoleate (PGPR) can be synthesised 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.
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    Solvent-free polyglycerol polyricinoleate synthesis mediated by lipase from Rhizopus arrhizus
    (2011-02-04) Gómez, J.L.; Bastida Rodríguez, Josefa; Máximo Martín, María Fuensanta; Montiel Morte, María Claudia; Murcia Almagro, María Dolores; Ortega Requena, Salvadora; Ingeniería Química