The Experts below are selected from a list of 309 Experts worldwide ranked by ideXlab platform

Sangho Koo - One of the best experts on this subject based on the ideXlab platform.

Fumiyuki Nakashio - One of the best experts on this subject based on the ideXlab platform.

  • enzymatic interesterification of triGlyceride with surfactant coated lipase in organic media
    Biotechnology and Bioengineering, 1995
    Co-Authors: Masahiro Goto, Muneharu Goto, Noriho Kamiya, Fumiyuki Nakashio
    Abstract:

    Several surfactant-coated enzymes have been prepared by coating lipases of various origins with a nonionic surfactant, glutamic acid dioleylester ribitol (2C18Δ9GE). Enzymatic interesterification of tripalmitin with oleic acid using the surfactant-coated lipase was carried out in organic media. The surfactant-coated lipases could effectively catalyze the interesterification of Glycerides better than did the powder lipases. A suitable organic solvent was an aliphatic hydrocarbon such as isooctane. The enzymatic activity for the interesterification strongly depended on the origin of the lipase. The surfactant-coated lipase prepared by Mucor javanicus showed the highest enzymatic activity for the interesterification of Glycerides, although its powder lipase did not show enzymatic activity. Selective interesterification of Glycerides could be performed by adjusting the concentration ratio of oleic acid to tripalmitin in isooctane. Di-substituted Glyceride could be selectively produced when the concentration ratio of carboxylic acid to Glycerides was 7. © 1995 John Wiley & Sons, Inc.

  • Enzymatic interesterification of triGlyceride with surfactant-coated lipase in organic media.
    Biotechnology and bioengineering, 1995
    Co-Authors: Masahiro Goto, Muneharu Goto, Noriho Kamiya, Fumiyuki Nakashio
    Abstract:

    Several surfactant-coated enzymes have been prepared by coating lipases of various origins with a nonionic surfactant, glutamic acid dioleylester ribitol (2C(18)Delta(9)GE). Enzymatic interesterification of tripalmitin with oleic acid using the surfactant-coated lipase was carried out in organic media. The surfactant-coated lipases could effectively catalyze the interesterification of Glycerides better than did the powder lipases. A suitable organic solvent was an aliphatic hydrocarbon such as isooctane. The enzymatic activity for the interesterification strongly depended on the origin of the lipase. The surfactant-coated lipase prepared by Mucor javanicus showed the highest enzymatic activity for the interesterification of Glycerides, although its powder lipase did not show enzymatic activity. Selective interesterification of Glycerides could be performed by adjusting the concentration ratio of oleic acid to tripalmitin in isooctane. Di-substituted Glyceride could be selectively produced when the concentration ratio of carboxylic acid to Glycerides was 7. (c) 1995 John Wiley & Sons, Inc.

Luis A Rios - One of the best experts on this subject based on the ideXlab platform.

  • maleinization of soybean oil Glycerides obtained from biodiesel derived crude glycerol
    Journal of the American Oil Chemists' Society, 2013
    Co-Authors: David A Echeverri, William A Perez, Luis A Rios
    Abstract:

    Glycerides obtained from the glycerolysis of soybean oil with crude glycerol were acylated with maleic anhydride at 80–100 °C. Both uncatalyzed and catalyzed reactions with 2-methylimidazole (2-MI) were evaluated. Formation of maleated Glycerides was confirmed by 1H-NMR and FTIR analyses. Consumption of maleic anhydride as a function of time was followed by acid value titration. High conversion (ca. 95 %) of hydroxyl groups was obtained at 90 °C in 60 min without catalyst. Under these conditions, a product with 1.9 maleate moieties per Glyceride molecule was obtained. Catalyzed reactions afforded lower conversions of hydroxyl groups and lower maleate yields compared to uncatalyzed reactions.

  • synthesis of maleated castor oil Glycerides from biodiesel derived crude glycerol
    Industrial Crops and Products, 2013
    Co-Authors: David A Echeverri, William A Perez, Luis A Rios
    Abstract:

    Abstract Castor oil Glycerides were obtained from the glycerolysis of castor oil or its methyl esters with alkaline-crude glycerol. High monoGlyceride yields were obtained between 20–30 min and 180–200 C with both substrates. The glycerolysis of castor oil afforded highest yield of products at 180 C and 30 min (50.4 of monoGlycerides and 35% of diGlycerides). However, the glycerolysis of methyl esters was more selective toward the formation of monoGlycerides. Castor oil Glycerides were further esterified with maleic anhydride without catalyst. Reaction was followed by acid value and 1H NMR. ca. 87% conversion of hydroxyl groups was obtained at 90 C. The final product contained 2.6 maleate groups per Glyceride molecule.

Bo Seul Choi - One of the best experts on this subject based on the ideXlab platform.

Masahiro Goto - One of the best experts on this subject based on the ideXlab platform.

  • enzymatic interesterification of triGlyceride with surfactant coated lipase in organic media
    Biotechnology and Bioengineering, 1995
    Co-Authors: Masahiro Goto, Muneharu Goto, Noriho Kamiya, Fumiyuki Nakashio
    Abstract:

    Several surfactant-coated enzymes have been prepared by coating lipases of various origins with a nonionic surfactant, glutamic acid dioleylester ribitol (2C18Δ9GE). Enzymatic interesterification of tripalmitin with oleic acid using the surfactant-coated lipase was carried out in organic media. The surfactant-coated lipases could effectively catalyze the interesterification of Glycerides better than did the powder lipases. A suitable organic solvent was an aliphatic hydrocarbon such as isooctane. The enzymatic activity for the interesterification strongly depended on the origin of the lipase. The surfactant-coated lipase prepared by Mucor javanicus showed the highest enzymatic activity for the interesterification of Glycerides, although its powder lipase did not show enzymatic activity. Selective interesterification of Glycerides could be performed by adjusting the concentration ratio of oleic acid to tripalmitin in isooctane. Di-substituted Glyceride could be selectively produced when the concentration ratio of carboxylic acid to Glycerides was 7. © 1995 John Wiley & Sons, Inc.

  • Enzymatic interesterification of triGlyceride with surfactant-coated lipase in organic media.
    Biotechnology and bioengineering, 1995
    Co-Authors: Masahiro Goto, Muneharu Goto, Noriho Kamiya, Fumiyuki Nakashio
    Abstract:

    Several surfactant-coated enzymes have been prepared by coating lipases of various origins with a nonionic surfactant, glutamic acid dioleylester ribitol (2C(18)Delta(9)GE). Enzymatic interesterification of tripalmitin with oleic acid using the surfactant-coated lipase was carried out in organic media. The surfactant-coated lipases could effectively catalyze the interesterification of Glycerides better than did the powder lipases. A suitable organic solvent was an aliphatic hydrocarbon such as isooctane. The enzymatic activity for the interesterification strongly depended on the origin of the lipase. The surfactant-coated lipase prepared by Mucor javanicus showed the highest enzymatic activity for the interesterification of Glycerides, although its powder lipase did not show enzymatic activity. Selective interesterification of Glycerides could be performed by adjusting the concentration ratio of oleic acid to tripalmitin in isooctane. Di-substituted Glyceride could be selectively produced when the concentration ratio of carboxylic acid to Glycerides was 7. (c) 1995 John Wiley & Sons, Inc.