Lipase immobilized on polydopamine-coated magnetite nanoparticles for biodiesel production from soybean oil

Andrade, Mauro; Parussulo, André L.A.; Netto, Caterina Gruenwaldt Cunha Marques; Andrade, Leandro H.; Toma, Henrique E.

doi:10.18331/brj2016.3.2.5

Cited by 58 publications

(20 citation statements)

References 21 publications

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“…The protein content before and after the immobilization process was determined to check the immobilization yield using Bradford's method. The formed nano-biocatalyst was washed several times with phosphate buffer to remove any unreacted lipase and then freeze dried [23,25].…”

Section: Lipase Immobilization On Modified Nanoparticlesmentioning

confidence: 99%

“…Xia also used RSM to optimize the enzymatic transesterification process, the optimum conditions reported are 4:1 methanol to oil ratio, 6.8% of biocatalyst and 42.2 • C reaction temperature [26]. Andrade et al used nano-biocatalyst prepared by immobilization of lipase on magnetic nano-particles and achieved the highest biodiesel yield at 4:1 methanol/oil raio, 20% enzyme conc., 37 • C temp., and 12 h of time period [25]. Andrade et al attained 95.5% methyl ester yield at 8:1 molar ratio of alcohol to oil, 8% biocatalyst amount and 45 • C temperature [48].…”

Section: Optimized Reaction Parametersmentioning

confidence: 99%

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Fe3O4-PDA-Lipase as Surface Functionalized Nano Biocatalyst for the Production of Biodiesel Using Waste Cooking Oil as Feedstock: Characterization and Process Optimization

et al. 2019

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Synthesis of surface modified/multi-functional nanoparticles has become a vital research area of material science. In the present work, iron oxide (Fe3O4) nanoparticles prepared by solvo-thermal method were functionalized by polydopamine. The catechol groups of polydopamine at the surface of nanoparticles provided the sites for the attachment of Aspergillus terreus AH-F2 lipase through adsorption, Schiff base and Michael addition mechanisms. The strategy was revealed to be facile and efficacious, as lipase immobilized on magnetic nanoparticles grant the edge of ease in recovery with utilizing external magnet and reusability of lipase. Maximum activity of free lipase was estimated to be 18.32 U/mg/min while activity of Fe3O4-PDA-Lipase was 17.82 U/mg/min (showing 97.27% residual activity). The lipase immobilized on polydopamine coated iron oxide (Fe3O4_PDA_Lipase) revealed better adoptability towards higher levels of temperature/pH comparative to free lipase. The synthesized (Fe3O4_PDA_Lipase) catalyst was employed for the preparation of biodiesel from waste cooking oil by enzymatic transesterification. Five factors response surface methodology was adopted for optimizing reaction conditions. The highest yield of biodiesel (92%) was achieved at 10% Fe3O4_PDA_Lipase percentage concentration, 6:1 CH3OH to oil ratio, 37 °C temperature, 0.6% water content and 30 h of reaction time. The Fe3O4-PDA-Lipase activity was not very affected after first four cycles and retained 25.79% of its initial activity after seven cycles. The nanoparticles were characterized by FTIR (Fourier transfer infrared) Spectroscopy, XRD (X-ray diffraction) and TEM (transmission electron microscopy), grafting of polydopamine on nanoparticles was confirmed by FTIR and formation of biodiesel was evaluated by FTIR and GC-MS (gas chromatography-mass spectrometry) analysis.

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Section: Lipase Immobilization On Modified Nanoparticlesmentioning

confidence: 99%

Section: Optimized Reaction Parametersmentioning

confidence: 99%

Fe3O4-PDA-Lipase as Surface Functionalized Nano Biocatalyst for the Production of Biodiesel Using Waste Cooking Oil as Feedstock: Characterization and Process Optimization

et al. 2019

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“…The synthesis of biodiesel by the transesterification of soybean oil catalyzed with BCL was also studied by Andrade, Parussulo, Netto, Andrade, and Toma (). In their report, the lipase was covalently immobilized on magnetic nanoparticles precoated with a thin layer of polydopamine.…”

Section: Synthesis Of Biodieselmentioning

confidence: 99%

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Sánchez

Tonetto

Ferreira

2017

Biotech & Bioengineering

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The lipase from Burkholderia cepacia, formerly known as Pseudomonas cepacia lipase, is a commercial enzyme in both soluble and immobilized forms widely recognized for its thermal resistance and tolerance to a large number of solvents and short-chain alcohols. The main applications of this lipase are in transesterification reactions and in the synthesis of drugs (because of the properties mentioned above). This review intends to show the features of this enzyme and some of the most relevant aspects of its use in different synthesis reactions. Also, different immobilization techniques together with the effect of various compounds on lipase activity are presented. This lipase shows important advantages over other lipases, especially in reaction media including solvents or reactions involving short-chain alcohols.

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“…The schematic diagram of covalent interaction between PGA and DMNF is shown in Figure 9. The reactive epoxide functional groups of glycidyl methacrylate can be directly covalent coupling the amino groups of PGA via ring opening reactions and polydopamine film could also offer an easy way to combine the amino groups of PGA by means of aldolic condensation or Schiff base reactions to enhance the structural rigidity and operational stability of PGA 28–29 …”

Section: Resultsmentioning

confidence: 99%

Di‐functional magnetic nanoflowers: A highly efficient support for immobilizing penicillin G acylase

Zheng

Xue

Shi

et al. 2020

J Chinese Chemical Soc

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The novel di-functional magnetic nanoflowers (DMNF) which had both epoxy groups and hydrophilic catechol as well as phthaloquinone groups capable of covalently coupling of penicillin G acylase (PGA) were characterized by scanning electron microscopy, transmission electron microscope (TEM), vibrating sample magnetometer, N 2 adsorption, and so on. The studies showed that DMNF possessed "hierarchical petal" structure of nanosheets had specific saturation magnetization of 39.7 emu/g and average pore diameter of 25.4 nm as well as specific surface area of 17.28 m 2 /g. For hydrolysis of penicillin G potassium catalyzed by the PGA immobilized on DMNF with enzyme loading of 106 mg/g-support, its apparent activity reached 2,667 U/g, which benefited from the "hierarchical petal" and large pore structure of the magnetic DMNF leading to high enzyme loading and fast diffusion of substrate molecules to the immobilized PGA to reaction. The apparent activity of the immobilized PGA could keep 2,408 U/g (above 90% of its initial activity) after repeating use for 10 cycles. The magnetic immobilized PGA exhibited excellent operational stability due to covalently coupling of the enzyme molecules between the support by covalent interaction of the amino groups of PGA and the reactive groups of epoxy, catechol, and phthaloquinone groups on DMNF. Furthermore, the PGA displayed good acid and alkaline resistance as well as thermal stability by immobilization using DMNF.

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Lipase immobilized on polydopamine-coated magnetite nanoparticles for biodiesel production from soybean oil

Cited by 58 publications

References 21 publications

Fe3O4-PDA-Lipase as Surface Functionalized Nano Biocatalyst for the Production of Biodiesel Using Waste Cooking Oil as Feedstock: Characterization and Process Optimization

Fe3O4-PDA-Lipase as Surface Functionalized Nano Biocatalyst for the Production of Biodiesel Using Waste Cooking Oil as Feedstock: Characterization and Process Optimization

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Di‐functional magnetic nanoflowers: A highly efficient support for immobilizing penicillin G acylase

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