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Bastida Rodríguez, Josefa

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Bastida Rodríguez, Josefa
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Universidad de Murcia. Departamento de Ingeniería Química
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  • Publication
    Open Access
    Biocatalytic synthesis of polymeric esters used as emulsifiers
    (Croatian Society of Chemical Engineers, 2019) Ortega Requena, Salvadora; Serrano-Arnaldos, M.; Montiel Morte, María Claudia; Máximo, María Fuensanta; Bastida Rodríguez, Josefa; Murcia Almagro, María Dolores; Ingeniería Química
    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 MP 64 by adsorption. The optimal immobilization conditions were determined: initial enzyme concentration of 13 mg of Lowry protein per mL phosphate buffer pH 7, and ricinoleic acid as a support activator. An immobilized derivative with 35.93 ± 4.90 mg of Lowry protein per g of dry support was obtained. It was used as a catalyst for PGPR production in open air and vacuum batch reactors, and the results obtained showed that 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).
  • Publication
    Restricted
    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.
  • Publication
    Open Access
    Understanding the enzymatic synthesis of a new biolubricant: decane-1,10-diyl bis(2-methylpentanoate)
    (MDPI, 2024-12-26) Ortega Requena, Salvadora; Máximo, María Fuensanta; Montiel Morte, María Claudia; Gómez Gómez, María; Murcia Almagro, María Dolores; Bastida Rodríguez, Josefa; Ingeniería Química; Facultades de la UMU::Facultad de Química
    The value of branched esters comes from the special properties they have in cold environments, which allow them to remain liquid over a wide range of temperatures. These properties make them useful for application in the cosmetic industry or as lubricant additives. This paper presents the studies carried out to ascertain the operational feasibility of the enzymatic esterification of 2-methylpentanoic acid (MPA) with 1,10-decanediol (DD), with the objective of obtaining a novel molecule: decane-1,10-diyl bis(2-methylpentanoate) (DDBMP). The enzymatic reaction is conducted in a thermostated batch reactor, utilizing the commercially available immobilized lipase Lipozyme® 435 in a solvent-free medium. The reaction conversion is determined by an acid number determination and a gas chromatographic analysis. The most optimal result is achieved at a temperature of 80 °C, a biocatalyst concentration of 2.5% (w/w), and a non-stoichiometric substrate relation. A preliminary economic study and the calculation of Green Metrics has established that the operation with a 30% molar excess of acid is the best option to obtain a product with 92.6% purity at a lower cost than the other options and in accordance with the 12 Principles of Green Chemistry. The synthetized diester has a viscosity index of 210, indicating that this new molecule can be used as a biolubricant at extreme temperatures.
  • Publication
    Open Access
    Guerbet alcohols, ideal substrates for the sustainable production of branched esters
    (MDPI, 2025-11-11) Montiel Morte, María Claudia; Máximo, María Fuensanta; Gómez Gómez, María; Murcia Almagro, María Dolores; Ortega Requena, Salvadora; Bastida Rodríguez, Josefa; Ingeniería Química; Facultad de Química
    Saturated and branched high molecular weight organic esters are highly valued as emollients in the cosmetic industry due to their superior properties. Their saturated character provides resistance to oxidation and rancidity. Additionally, their branched structure endows them with low melting temperatures, enabling them to remain liquid over a broad temperature range. These esters can be obtained from branched alcohols, branched fatty acids or both, using chemical or enzymatic processes. Among branched alcohols, Guerbet alcohols stand out. Due to their characteristic properties as branched, saturated alcohols with superior oxidative stability and extremely low volatility, they are proposed as excellent substrates for the enzymatic synthesis of these compounds. This study represents the first investigation into the biocatalytic synthesis of three specific esters: those formed between 2-octyl-1-dodecanol (C20 Guerbet alcohol) and the fatty acids myristic (MA), palmitic (PA), and stearic acid (SA). To achieve this, an environmentally sustainable biocatalytic process was developed. The synthesis involves a solvent-free esterification catalyzed by the commercial immobilized lipase, Lipozyme® 435, conducted within a vertically stirred, thermostated batch tank reactor. Optimal conditions for lipase concentration and temperature were established, and the sustainability of the process was successfully quantified using various “green metrics”.