Lipase coated clusters of iron oxide nanoparticles for biodiesel synthesis in a solvent free medium

Mukherjee, Jaya; Gupta, Munishwar N.

doi:10.1016/j.biortech.2016.02.134

Cited by 27 publications

(9 citation statements)

References 30 publications

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“…From the examples presented in Table 7, the time needed to attain reaction equilibrium is between 0.5 to 120 h. longer reaction times reflect on a lower biodiesel productivity, which can be easily calculated from these examples. The highest FAEEs productivity (33 % FAEEs/h) was obtained by ethanolysis of soybean oil catalyzed by Thermomyces lanuginosa lipase immobilized on iron oxide nanoparticles [189] followed by 19 % FAEEs/h when Lipozyme TL IM was used [190]. In methanolysis, in hexane medium, the highest productivity value (154 % FAMEs/h) [191] followed by 19 % FAMEs/h [78] were attained with Lipozyme RM IM as catalyst.…”

Section: Immobilized Lipasesmentioning

confidence: 99%

“…The sn-1,3 regioselective Thermomyces lanuginosa lipase was immobilized on iron oxide nanoparticles, to facilitate biocatalyst recovery with a magnet, and used in the presence of silica to facilitate acyl migration and promote FAMEs synthesis [189]. Also, the use of Amberlite IRA-93 resin, to immobilize the sn-1,3 regioselective recombinant R. oryzae lipase, showed to accelerate acyl migration allowing the conversion of TAG into FAMEs and glycerol [186].…”

Section: Immobilized Lipasesmentioning

confidence: 99%

“…"Ecodiesel" is a glycerol-free biodiesel. This novel biofuel containing FAMEs/MAG or FAEEs/MAG blends presented similar physical properties to those of conventional biodiesel[219].However, when sn-1,3 regioselective lipases are used and a maximum conversion of oil into FAMEs is desired, acyl migration can be promoted by the presence of silica in the reaction medium ([189];…”

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confidence: 96%

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Enzyme-Catalyzed Production of Biodiesel as Alternative to Chemical- Catalyzed Processes: Advantages and Constraints

Sandoval

Casas-Godoy

Bonet-Ragel

et al. 2017

CBE

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Biodiesel represents an interesting alternative to fossil fuels. Traditionally the standard method for biodiesel production from oils is alkaline-catalyzed transesterification. Chemical catalysis can be replaced by enzymatic catalysis using lipases (EC 3.1.1.3, triacylglycerol acyl hydrolases), obtained from plants, animals or microorganisms. These biocatalysts act at milder temperature and normal pressure conditions, resulting in lower energy consumption. Also, undesirable side-reactions do not occur, originating pure products. Refined vegetable oils are the most common feedstocks for biodiesel production, accounting for 70-80% of the overall biodiesel production costs. The search for low-cost feedstocks, i.e. non-edible oils and high acidic waste oils/greases, is an alternative to make biodiesel competitive. Non-regioselective and sn-1,3regioselective lipases can catalyze esterification of free fatty acids and transesterification of triacylglycerols with good yields. The lipases used as catalysts for biodiesel production must present alcohol resistance, thermo-tolerance, high stability and activity. Recently, enzymatic processes for biodiesel production have been implemented at industrial scale. Despite this trend, the conventional chemical process still remains the most popular, mainly due to the high cost of commercial lipases. This review consists of an update of the state of the art of enzymatic biodiesel production, including legislation, feedstocks, lipases used for biodiesel synthesis, the role of acyl acceptors and strategies to avoid lipase inactivation, the mechanisms proposed for biocatalysis and the enzymatic bioreactors used. In addition, the economics of the bioprocess is also presented.

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Section: Immobilized Lipasesmentioning

confidence: 99%

Section: Immobilized Lipasesmentioning

confidence: 99%

mentioning

confidence: 96%

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Enzyme-Catalyzed Production of Biodiesel as Alternative to Chemical- Catalyzed Processes: Advantages and Constraints

Sandoval

Casas-Godoy

Bonet-Ragel

et al. 2017

CBE

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“…Hydrophobic enzyme reactions normally contain an antinomy. A fatty acid substrate needs a hydrophobic solvent [14][15][16]. However, enzymes dislike hydrophobic surroundings as they require a certain amount of water molecules to form a special molecular structure for reactivity.…”

Section: Introductionmentioning

confidence: 99%

Promising Immobilization of Industrial-Class Phospholipase A1 to Attain High-Yield Phospholipids Hydrolysis and Repeated Use with Optimal Water Content in Water-in-Oil Microemulsion Phase

et al. 2021

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In this study, we maximized the reactivity of phospholipids hydrolysis with immobilized industrial-class phospholipase A1 (PLA1) at the desired water content in the water-in-oil (W/O) microemulsion phase. The optimal hydrophobic-hydrophilic condition of the reaction media in a hydrophobic enzyme reaction is critical to realize the maximum yields of enzyme activity of phospholipase A1. It was attributed to enzymes disliking hydrophobic surroundings as a special molecular structure for reactivity. Immobilization of PLA1 was successfully achieved with the aid of a hydrophobic carrier (Accurel MP100) combination with the treatment using glutaraldehyde. The immobilized yield was over 90% based on simple adsorption. The hydrolysis reaction was kinetically investigated through the effect of glutaraldehyde treatment of carrier and water content in the W/O microemulsion phase. The initial reaction rate increased linearly with an increasing glutaraldehyde concentration and then leveled off over a 6% glutaraldehyde concentration. The initial reaction rate, which was predominantly driven by the water content in the organic phase, changed according to a typical bell-shaped curve with respect to the molar ratio of water to phospholipid. It behaved in a similar way with different glutaraldehyde concentrations. After 10 cycles of repeated use, the reactivity was well sustained at 40% of the initial reaction rate and the creation of the final product. Accumulated yield after 10 times repetition was sufficient for industrial applications. Immobilized PLA1 has demonstrated potential as a biocatalyst for the production of phospholipid biochemicals.

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“…22 In general, increasing the hydrophobicity of the surface in the immediate area surrounding the active site, exposing a large hydrophobic area which can interact with the hydrophobic interface and the catalytic triad becomes accessible to the hydrophobic substrate. [25][26][27][28][29][30] It is expected that hydrophobic carriers would provide more access of the substrate to the active site of the immobilized lipase.…”

Section: Introductionmentioning

confidence: 99%

Improved performance of immobilized lipase by interfacial activation on Fe₃O₄@PVBC nanoparticles

2017

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Lipase coated clusters of iron oxide nanoparticles for biodiesel synthesis in a solvent free medium

Cited by 27 publications

References 30 publications

Enzyme-Catalyzed Production of Biodiesel as Alternative to Chemical- Catalyzed Processes: Advantages and Constraints

Enzyme-Catalyzed Production of Biodiesel as Alternative to Chemical- Catalyzed Processes: Advantages and Constraints

Promising Immobilization of Industrial-Class Phospholipase A1 to Attain High-Yield Phospholipids Hydrolysis and Repeated Use with Optimal Water Content in Water-in-Oil Microemulsion Phase

Improved performance of immobilized lipase by interfacial activation on Fe₃O₄@PVBC nanoparticles

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Lipase coated clusters of iron oxide nanoparticles for biodiesel synthesis in a solvent free medium

Cited by 27 publications

References 30 publications

Enzyme-Catalyzed Production of Biodiesel as Alternative to Chemical- Catalyzed Processes: Advantages and Constraints

Enzyme-Catalyzed Production of Biodiesel as Alternative to Chemical- Catalyzed Processes: Advantages and Constraints

Promising Immobilization of Industrial-Class Phospholipase A1 to Attain High-Yield Phospholipids Hydrolysis and Repeated Use with Optimal Water Content in Water-in-Oil Microemulsion Phase

Improved performance of immobilized lipase by interfacial activation on Fe3O4@PVBC nanoparticles

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Improved performance of immobilized lipase by interfacial activation on Fe₃O₄@PVBC nanoparticles