Browsing by Subject "Estolide"

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    ENZYMATIC BIOSYNTHESIS OF RICINOLEIC ACID ESTOLIDES
    (Elsevier, 2005-05-31) Bódalo-Santoyo, A.; Bastida Rodríguez, Josefa; Máximo Martín, María Fuensanta; Montiel Morte, María Claudia; Murcia Almagro, María Dolores; Ingeniería Química
    Candida rugosa lipase has been shown to have sufficient activity to catalyse the enzymatic synthesis of ricinoleic acid estolides in a batch reactor. The water requirements of the reactor change during the reaction: at the beginning of the process a minimum amount of water is necessary but, later, the reaction mixture must be dried out to obtain an estolide with a high degree of condensation. The influence on the reaction rate of variables, such as water content, enzyme concentration and mixing devices, was established and optimised. Using an initial water content of 144000 ppm and a lipase concentration of 13.33 mgE/g ricin, and maintaining the temperature at 40°C by mean of hot air circulation and using a three-bladed propeller stirrer as mixing device, an estolide of ricinoleic acid with an acid number of 65 was obtained in 48 hours.
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    PRODUCTION OF RICINOLEIC ACID ESTOLIDE WITH FREE AND IMMOBILIZED LIPASE FROM Candida rugosa.
    (2007-10-23) Bódalo, A.; Bastida Rodríguez, Josefa; Máximo Martín, María Fuensanta; Montiel Morte, María Claudia; Gómez, M.; Murcia Almagro, María Dolores; Ingeniería Química
    Ricinoleic acid estolide was produced by using free and immobilized Candida rugosa lipase at moderate temperature in a bioreactor. This work describes the immobilization of Candida rugosa lipase on ten different supports by covalent binding and physical adsorption, and how of the most suitable immobilized derivative was selected. The comparison was mainly based on the enzyme content and on the activity results. An anion exchange resin was judged to be the most appropriate support and the corresponding immobilization process was investigated and optimized. Although repeated batch reactions using the same derivative are not entirely advisable, the reaction proceeds at a noticeably slower rate and the degree of condensation reached is lower when the same amount of protein as in the derivative is added to the bioreactor in native form.