Solvent-free polyglycerol polyricinoleate synthesis mediated by lipase from Rhizopus arrhizus

Bastida, Jaume; Máximo, M.F.; Montiel, M.C.; Murcia, M.D.; Ortega, S.

doi:10.1016/j.bej.2011.02.007

Cited by 27 publications

(38 citation statements)

References 12 publications

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“…is fact, together with the high operating temperature, can adversely affect the quality of the �nal product because of problems related with coloration and odours, making it unsuitable for the food industry [57]. As an alternative, a biocatalytic synthesis of PGPR using enzymes has been recently proposed by the author research group [61][62][63][64][65][66]. Lipases are able to act in mild reaction conditions and produce a �nal product more suitable for use as a food additive.…”

Section: Enzymaticmentioning

confidence: 99%

The Food Additive Polyglycerol Polyricinoleate (E-476): Structure, Applications, and Production Methods

Bastida

2013

ISRN Chemical Engineering

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e food additive named polyglycerol polyricinoleate (PGPR) and identi�ed with the code E-476 (PGPR) is used as emulsi�er 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, besides its action as an emulsi�er, it also has important properties as a viscosity modi�er and thus improves the moulding properties of the molten chocolate. An additional property of PGPR in chocolate is its ability to limit fat bloom. �nown chemical methods for preparing this emulsi�er involve long reaction times and high operating temperatures, which adversely affect the quality of the �nal product leading to problems of coloration and odors that could make it inadvisable for the food industry. As an alternative, the enzymatic synthesis of PGPR by the catalytic action of two lipases has been developed. e enzymes act in mild reaction conditions of temperature and pressure, neutral pH, and in a solvent-free system, which makes the process environmentally friendly and avoids side reaction, so that the product has a higher purity and quality.

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Section: Enzymaticmentioning

confidence: 99%

The Food Additive Polyglycerol Polyricinoleate (E-476): Structure, Applications, and Production Methods

Bastida

2013

ISRN Chemical Engineering

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“…PDI values remained low throughout the time course of reaction, residing between 1.1 and 1.2. Further research is needed to determine if the percent incorporation of undecenoic acid can be increased without increasing the final FFA concentration, perhaps by adding undecenoic acid into the reaction mixture in small batchwise increments throughout the time course of reaction, and/or by applying a more effective means of water removal than free evaporation, such as high vacuum pressure [7,8]. (It is known that the small amount of non-hydroxy fatty acid present in technical grade ricinoleic acid is readily incorporated as end groups for oligo-ricinoleic acid [9], suggesting the former approach may be successful.)…”

Section: Cal-catalyzed Esterification Of Oligo-ricinoleic Acid and 10mentioning

confidence: 99%

“…Chromatographic analyses demonstrate the reaction between PGPR (prepared using lipases under solvent-free conditions [7,8]) and undecenoic acid greatly affected the chemical nature of the polymer (Figure 2). Normal phase HPLC provided the more useful data for interpretation, demonstrating the existence of two main bands for the starting material, a main and broad band between 3.0 and 4.5 min retention time and a second sharper band at 4.5-5.0 min.…”

Section: Cal-catalyzed Esterification Of Polyglyerol Polyricinoleate mentioning

confidence: 99%

“…In addition, polyglycerol polyricinoleate, PGPR, consisting of oligo-ricinoleic acid chains grafted onto polyglycerol via ester bond formation, is a well-known biobased and biocompatible emulsifier for foods and pharmaceuticals [5][6][7]. oligo-Ricinoleic acid and its derivatives (including PGPR [8]) are readily formed using lipases under nonaqueous media and moderate operating conditions; e.g., 50-80 °C and near-ambient pressure [9]. Reviewed elsewhere, enzymes, particularly lipases, are potentially valuable biocatalysts for catalyzing polymer synthesis, providing a "green" manufacturing route to polymer synthesis, and imparting unique selectivity toward polymerization, including the preparation of optically pure polymers (reviewed in [10][11][12][13][14][15]).…”

Section: Introductionmentioning

confidence: 99%

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Modification of oligo-Ricinoleic Acid and Its Derivatives with 10-Undecenoic Acid via Lipase-Catalyzed Esterification

Hayes

Mannam

et al. 2012

Polymers

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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. OPEN ACCESSPolymers 2012, 4 1038

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“…However, the drawbacks of soluble enzymes are their instability, easy deactivation and generation of secondary pollution after their reuse. Therefore, the technology of immobilized enzymes is introduced to overcome the disadvantages and enable simpler separation, recyclability and reutilization, while it also enhances thermal, pH and storage stability (Moradzadegan et al, 2010;Gómez et al, 2011;Fernández-Fernández et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Characterization and optimization of mesoporous magnetic nanoparticles for immobilization and enhanced performance of porcine pancreatic lipase

et al. 2015

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In this paper, Fe3O4 nanoparticles coated with mesoporous silica were prepared successfully, noted as Fe3O4 at the mobile composition of matter No. 41 (MCM-41). Also, Fe3O4 at MCM-41 was grafted by both 3-aminopropyltriethoxysilane (APTS) and 3-chloropropyltriethoxysilane (CPS), noted as Fe3O4 at MCM-41/APTS and Fe3O4 at MCM-41/CPS. The compounds were characterized by X-ray powder diffraction, scanning electron microscopy, transmission electron microscopy, Fourier transform infrared spectroscopy, vibrating sample magnetometry, thermogravimetry and N2 adsorption/desorption. Then, the enzyme, porcine pancreas lipase (PPL), was immobilized onto these modified nanoparticles by covalent attachment, physical adsorption and cross-linking, noted as Fe3O4 at MCM-41/CPS-PPL, Fe3O4 at MCM-41-PPL and Fe3O4 at MCM-41/APTS-PPL, respectively. The results showed that Fe3O4 at MCM-41/CPS was the best nanomaterial for PPL immobilization, exhibiting enhanced immobilization efficiency (maximum 96 %), maximum relative activity (up to 96 %), high stability and reusability (83 % 56 days and 86.7 % ten cycles). Additionally, it offered some other advantages, such as easy recycling and reuse, complying with the trend of green chemistry. Therefore, Fe3O4 at MCM-41/CPS in combination with a relevant method can be proposed for commercial applications.

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Solvent-free polyglycerol polyricinoleate synthesis mediated by lipase from Rhizopus arrhizus

Cited by 27 publications

References 12 publications

The Food Additive Polyglycerol Polyricinoleate (E-476): Structure, Applications, and Production Methods

The Food Additive Polyglycerol Polyricinoleate (E-476): Structure, Applications, and Production Methods

Modification of oligo-Ricinoleic Acid and Its Derivatives with 10-Undecenoic Acid via Lipase-Catalyzed Esterification

Characterization and optimization of mesoporous magnetic nanoparticles for immobilization and enhanced performance of porcine pancreatic lipase

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