Immobilized lipase-catalyzed esterification for synthesis of trimethylolpropane triester as a biolubricant

Kim, Heejin; Choi, Nakyung; Kim, Yangha; Kim, Hak Ryul; Lee, Junsoo; Kim, In Hwan

doi:10.1016/j.renene.2018.06.092

Cited by 54 publications

(19 citation statements)

References 26 publications

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“…42 The heterogeneity of the natural substrate [43][44][45][46][47][48] has converted lipases in enzymes with a very broad specificity, accepting substrates very different from glycerides (even amides). Thus, lipases are used in vitro to catalyze reactions different from those of the natural hydrolase function, [49][50][51][52][53][54] such as esterification, [55][56][57][58][59][60][61] acidolysis, [62][63][64][65][66][67] interesterificaton, [68][69][70][71] transesterification, [72][73][74][75][76] aminolysis, [77][78][79][80][81] perhydrolysis, 82,83 etc., together with a collection of the so-called promiscuous reactions. [84][85][86][87][88]...…”

Section: Lipases In Biocatalysismentioning

confidence: 99%

Novozym 435: the “perfect” lipase immobilized biocatalyst?

Ortíz

Ferreira

Barbosa

et al. 2019

Catal. Sci. Technol.

471

360

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Section: Lipases In Biocatalysismentioning

confidence: 99%

Novozym 435: the “perfect” lipase immobilized biocatalyst?

Ortíz

Ferreira

Barbosa

et al. 2019

Catal. Sci. Technol.

471

360

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“…Among the most used enzymes, lipases stand out [42,43]. The natural function of lipases is the hydrolysis of triglycerides to free fatty acids and glycerol [44]; however, in vitro lipases have been used in a wide variety of reactions, some related to oil modifications (esterifications [45][46][47][48][49][50][51], transesterifications [52][53][54][55][56], acidolysis [57][58][59][60][61][62], interesterifcations [63][64][65][66]), some far from these substrates (resolution of racemic mixtures, regio or enantio selective reactions) and some have even exhibited a diversity of the so-called promiscuous activities far from their natural function [67][68][69][70][71][72][73][74][75].…”

Section: Lipases In Biocatalysismentioning

confidence: 99%

Lecitase ultra: A phospholipase with great potential in biocatalysis

Virgen-Ortíz

Santos

Ortíz

et al. 2019

Molecular Catalysis

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Lecitase Ultra is a chimera produced by the fusion of the genes of the lipase from Thermomyces lanuginosus and the phospholipase A1 from Fusarium oxysporum. The enzyme was first designed for the enzymatic degumming of oils, as that problem was not fully resolved before. It is commercialized only as an enzyme solution by Novo Nordisk A/S. This review shows the main uses of this promising enzyme. Starting from the original degumming use, the enzyme has found applications in many other food modification applications, like production of structured phospholipids (e.g., derivatives of phosphatidylcholine), tuning the properties of flour, etc. Moreover, the enzyme has been used in fine chemistry (resolution of racemic mixtures), in the production of aromas and fragrances, polymers modification, etc. Some papers show the use of the enzyme in biodiesel production. Moreover, we present the different technologies applied to obtain a suitable immobilized biocatalyst, remarking the immobilization via interfacial activation and how heterofunctional acyl supports may solve some of the limitations. Immobilized enzyme physical and chemical modifications have also been presented. Finally, Lecitase Ultra has been one of the model enzymes in a new strategy to coimmobilize lipases and other less stable enzymes.

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“…In addition, TLL has been successfully applied in the production of synthetic biolubricants. Similar conversions (about 90%) of synthetic biolubricants were obtained using TLL immobilized on different solid supports, such as citric acid-modified magnetite nanoparticles [ 8 ], Duolite A568 [ 17 ], and mesoporous hydrophobic poly-methacrylate [ 3 , 16 ].…”

Section: Introductionmentioning

confidence: 69%

“…Synthetic biolubricants are obtained by direct esterification of fatty acids [ 16 , 17 ], transesterification between monoalkyl esters of the target fatty acid or glycerides and the desired alcohol [ 18 , 19 ], or hydroesterification, a sequential process of hydrolysis of oils/fats followed by esterification of the purified fatty acids [ 1 , 8 ]. These reactions have been performed using either homogeneous or heterogeneous catalysts, however, from an industrial point of view, heterogeneous catalysts are preferred due to the easier recovery of the catalyst and lower generation of chemical wastes [ 20 ].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Eversa® Transform via CLEA Technology Converts It in a Suitable Biocatalyst for Biolubricant Production Using Waste Cooking Oil

et al. 2021

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The performance of the previously optimized magnetic cross-linked enzyme aggregate of Eversa (Eversa-mCLEA) in the enzymatic synthesis of biolubricants by transesterification of waste cooking oil (WCO) with different alcohols has been evaluated. Eversa-mCLEA showed good activities using these alcohols, reaching a transesterification activity with isoamyl alcohol around 10-fold higher than with methanol. Yields of isoamyl fatty acid ester synthesis were similar using WCO or refined oil, confirming that this biocatalyst could be utilized to transform this residue into a valuable product. The effects of WCO/isoamyl alcohol molar ratio and enzyme load on the synthesis of biolubricant were also investigated. A maximum yield of around 90 wt.% was reached after 72 h of reaction using an enzyme load of 12 esterification units/g oil and a WCO/alcohol molar ratio of 1:6 in a solvent-free system. At the same conditions, the liquid Eversa yielded a maximum ester yield of only 34%. This study demonstrated the great changes in the enzyme properties that can be derived from a proper immobilization system. Moreover, it also shows the potential of WCO as a feedstock for the production of isoamyl fatty acid esters, which are potential candidates as biolubricants.

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Immobilized lipase-catalyzed esterification for synthesis of trimethylolpropane triester as a biolubricant

Cited by 54 publications

References 26 publications

Novozym 435: the “perfect” lipase immobilized biocatalyst?

Novozym 435: the “perfect” lipase immobilized biocatalyst?

Lecitase ultra: A phospholipase with great potential in biocatalysis

Immobilization of Eversa® Transform via CLEA Technology Converts It in a Suitable Biocatalyst for Biolubricant Production Using Waste Cooking Oil

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