Highly active and stable Fe3O4/Au nanoparticles supporting lipase catalyst for biodiesel production from waste tomato

Sarno, Maria; Iuliano, Mariagrazia

doi:10.1016/j.apsusc.2018.04.060

Cited by 78 publications

(39 citation statements)

References 64 publications

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“…In this case, the enzymatic activity recovery was shown to increase from 34.1% to 63.5% by enhancing the lipase concentration from 1.0 mg/mL to 2.0 mg/mL; however, further increment in the lipase concentration beyond 2.0 mg/mL led to decreased activity recovery. A similar phenomenon has also been observed in several previous studies [12,[33][34][35]. At a low lipase concentration, the low activity recovery was attained owing to less amounts of bound lipase.…”

Section: Factors Affecting the Immobilization Efficiency And Enzymatisupporting

confidence: 88%

“…However, the covalent bonds between the enzyme and the magnetic support could lead to the stabilization of the configuration for the bound lipase and the improvement of its stability. Considering the reusability study, the long-term stability for the immobilized lipase is really comparable to that reported in the previous work [19,23,[33][34][35].…”

Section: Reusability Of the Immobilized Lipasesupporting

confidence: 85%

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Enzymatic Production of Biodiesel Using Immobilized Lipase on Core-Shell Structured Fe3O4@MIL-100(Fe) Composites

Xie

Huang

2019

Catalysts

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In this research, core–shell structured Fe3O4@MIL-100(Fe) composites were prepared by coating Fe3O4 magnetite with porous MIL-100(Fe) metal-organic framework (MOF) material, which were then utilized as magnetic supports for the covalent immobilization of the lipase from Candida rugosa through amide linkages. By using the carbodiimide/hydroxysulfosuccinimide (EDC/NHS) activation strategy, the lipase immobilization efficiency could reach 83.1%, with an activity recovery of 63.5%. The magnetic Fe3O4@MIL-100(Fe) composite and immobilized lipase were characterized by several techniques. The characterization results showed that the Fe3O4 core was coated with MIL-100(Fe) shell with the formation of perfect core–shell structured composites, and moreover, the lipase was covalently tethered on the magnetic carrier. The immobilized lipase displayed a strong magnetic response and could be facilely separated by an external magnetic field. With this magnetic biocatalyst, the maximum biodiesel conversion attained 92.3% at a methanol/oil molar ratio of 4:1, with a three-step methanol addition manner, and a reaction temperature of 40 °C. Moreover, the biocatalyst prepared in the present study was recycled easily by magnetic separation without significant mass loss, and displayed 83.6% of its initial activity as it was reused for five runs, thus allowing its potential application for the cleaner production of biodiesel.

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Section: Factors Affecting the Immobilization Efficiency And Enzymatisupporting

confidence: 88%

Section: Reusability Of the Immobilized Lipasesupporting

confidence: 85%

Enzymatic Production of Biodiesel Using Immobilized Lipase on Core-Shell Structured Fe3O4@MIL-100(Fe) Composites

Xie

Huang

2019

Catalysts

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Section: Synthesis Of Fe 3 O 4 /Au Nps Ligand Exchange To Obtain Hydmentioning

confidence: 99%

“…The Fe 3 O 4 /Au@OA nanoparticles were prepared as previously reported [24]. In particular, two diefferent samples were prepared increasing the amount of Au NPs precursor (HAuCl 4 ) from 42 mg to 62 mg. For the immobilization, optimized conditions [24] were chosen. In particular, modified NPs were mixed [24] with 10 mL of buffer solution (phosphate buffer 0.1 M, to give at pH = 3.0) with 2 mg of TL (solution ≥ 100,000 U/g from Sigma Aldrich) and shaken at 200 rpm, T = 4°C, for 180 min, obtaining TL immobilized lipase, named NPs@TL in the following.…”

Section: Synthesis Of Fe 3 O 4 /Au Nps Ligand Exchange To Obtain Hydmentioning

confidence: 99%

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Biodiesel production from waste cooking oil

Sarno

Iuliano

2019

Green Processing and Synthesis

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Biodiesel production from waste cooking oil was obtained using Thermomyces lanuginosus (TL) lipase (E.C.3.1.1.3) anchored on Fe3O4/Au nanoparticles through physical interactions. A remarkable biodiesel yield of ∼90% was obtained without any pre-treatment and at a lipase concentration of 20%, 45°C reaction temperature, 1:6 oil/methanol molar ratio, after 24 h. The immobilized enzyme showed fast kinetic (the biodiesel yield was already of 34.6% after only 3 h) and activity slightly dependent on the length of the acid chains. The effect of the Au NPs sizes was monitored, to study the role of Au conduction centres in facilitating enzymes favourable orientation. The immobilized lipase activity stays above 74% after the first 3 cycles of use. In particular, the produced biodiesel presents an ester content of 97.8% ± 0.21 and a linolenic methyl ester content of 0.53% ± 0.03, in agreement with EN14214 requirements.

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Lipase‐Immobilized Magnetic Nanoparticles: Promising Nanobiocatalysts for Biodiesel Production

Touqeer

Mumtaz

Mukhtar

2021

Nano‐ and Biocatalysts for Biodiesel Production

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Highly active and stable Fe3O4/Au nanoparticles supporting lipase catalyst for biodiesel production from waste tomato

Cited by 78 publications

References 64 publications

Enzymatic Production of Biodiesel Using Immobilized Lipase on Core-Shell Structured Fe3O4@MIL-100(Fe) Composites

Enzymatic Production of Biodiesel Using Immobilized Lipase on Core-Shell Structured Fe3O4@MIL-100(Fe) Composites

Biodiesel production from waste cooking oil

Lipase‐Immobilized Magnetic Nanoparticles: Promising Nanobiocatalysts for Biodiesel Production

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