Nanobioconjugates of Candida antarctica lipase B and single-walled carbon nanotubes in biodiesel production

Bencze, László Csaba; Bartha-Vári, Judith H.; Katona, Gabriel; Toşa, Monica Ioana; Paizs, Csaba; Irimie, Florin Dan

doi:10.1016/j.biortech.2015.10.072

Cited by 71 publications

(33 citation statements)

References 33 publications

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“…This was attributed to the suitable volume of organic solvent that can promote mass transfer of the substrates to active sites of the lipase. However, excess organic solvent will lead to decrease of the substrate concentration and then reduced yield . Thus, n‐hexane and a substrate–solvent ratio of 1:2 (w/v) were chosen for the subsequent reactions.…”

Section: Resultsmentioning

confidence: 99%

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Lipase based static emulsions as efficient biocatalysts for biodiesel production

Zhou

Jiang

et al. 2016

J of Chemical Tech & Biotech

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BACKGROUND Enzymatic production of biodiesel is an alternative solution to circumvent the problems associated with chemical catalysis. However, the drawbacks, including lower stability and reusability of the lipase, often make this route unfeasible for industrial application. RESULTS A stable biocatalyst system was prepared by trapping an aqueous solution of Burkholderiacepacia lipase (BCL) in bead‐shaped silicone microspheres (named lipase‐based static emulsions). Compared with free BCL, lipase‐based static emulsions showed outstanding stability under vigorous shaking conditions and the thermal stability was improved. The lipase‐based static emulsions were employed to catalyze the transesterification of soybean oil with ethanol for biodiesel production. Under the optimum conditions, about 95.42% of FAEE yield was achieved in 30 h. In addition, the lipase‐based static emulsions presented good reusability, and the FAEE yield remained at more than 70.63% after 15 successive reaction cycles. The lipase‐based static emulsions were also used to catalyze the transesterification of jatropha oil and cottonseed oil with ethanol for biodiesel production, and the maximum FAEE yield was 96.10% and 90.39%, respectively. CONCLUSIONS Lipase‐based static emulsions were developed as robust biocatalysts by trapping an aqueous solution of lipase in silicone microspheres. The lipase‐based static emulsions catalyzed process may be a suitable technique for biodiesel production. © 2016 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 99%

“…However, excess organic solvent will lead to decrease of the substrate concentration and then reduced yield. 4, 35 Thus, n-hexane and a substrate-solvent ratio of 1:2 (w/v) were chosen for the subsequent reactions.…”

Section: Biodiesel Production Catalyzed By the Lipase-based Static Emmentioning

confidence: 99%

Lipase based static emulsions as efficient biocatalysts for biodiesel production

Zhou

Jiang

et al. 2016

J of Chemical Tech & Biotech

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“…Since lipase B from Candida antarctica covalently immobilized on carboxylated single-walled carbon nanotubes (SwCNT COOH ) proved to be a highly efficient biocatalyst for biodiesel synthesis [36], and Amano lipase from Pseudomonas fluorescens (L-AK) shows an unusually high methanol and ethanol resistance, being efficient in biodiesel production [37] even after its immobilization on hydrophobic supports by adsorption [38], the present study aims to develop a novel, highly active and stable biocatalyst for the conversion of sunflower oil into the corresponding FAEE through the covalent immobilization of L-AK on various hydrophobic carbon nanomaterial supports (carboxy and amino-functionalized single-walled carbon nanotubes (SwCNT COOH and SwCNT NH2 ), and reduced graphene oxide (rGO)) of large surface area, derivatized with various linkers with different lengths.…”

Section: Introductionmentioning

confidence: 99%

Efficient Biodiesel Production Catalyzed by Nanobioconjugate of Lipase from Pseudomonas fluorescens

et al. 2020

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The Amano lipase from Pseudomonas fluorescens (L-AK) was covalently immobilized on various carbon nanomaterials (functionalized single-walled carbon nanotubes and graphene oxide) and tested for biodiesel production. Using the most active lipase preparation (covalently immobilized L-AK on SwCNTNH2 derivatized with glycerol diglycidyl ether) under optimal conditions, quasi-complete conversion (>99%) of sunflower oil was obtained after only 4 h reaction time. Moreover, the biocatalyst maintained more than 99% of its initial activity in the batch system after multiple recycling experiments.

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“…lipase from Burkholderia cepacia, formerly known as Pseudomonas cepacia lipase (Lipase PS), 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 [43]. The main applications of this lipase are in transesterification reactions [44,45] and in the synthesis of drugs. This enzyme is a widely applied for highly enantiomer selective resolution of racemic primary and secondary alcohols [46][47][48][49].…”

Section: Introductionmentioning

confidence: 99%

Bisepoxide-activated Hollow Silica Microspheres for Covalent Immobilization of Lipase from Burkholderia cepacia

Nagy

Szabó

Bugovics

et al. 2019

Period. Polytech. Chem. Eng.

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An efficient and easy-to-perform method was developed for covalent immobilization of lipase from Burkholderia cepacia (Lipase PS) on hollow silica microspheres (M540) by bisepoxide activation. For immobilization, various bisepoxides of different length, rigidity and hydrophobicity in their linkers were applied to activate the amino groups on the M540 support. Effect of the individual bisepoxides on the catalytic performance of the immobilized Lipase PS was studied by using lipase-catalyzed kinetic resolution (KR) of racemic 1-phenylethanol (rac-1) with vinyl acetate in batch mode. Catalytic activity, enantiomer selectivity, recyclability and thermal stability of the new immobilized Lipase PS biocatalysts were investigated. The optimal enzyme / support ratio with the support activated by the most efficient bisepoxide, i.e. poly(ethylene glycol) diglycidyl ether (PDE), was 1:5. The most efficient Lipase PS on PDE activated M540 showed an almost five fold higher biocatalytic activity value (rbatch = 42.8 U/g) with enhanced selectivity (ee(R)-2 = 99.1 %) to the free form of Lipase PS (rbatch = 9.0 U/g; ee(R)-2 = 98.9 %). The Lipase PS on PDE-M540 was compared to a commercially available immobilized Lipase PS biocatalyst (Lipobond Lipase PS) and also applied in a packed-bed enzyme reactor operated in continuous-flow mode, where the optimal temperature of M540-PDE-PS reached the 70 °C, while the optimum for Lipobond Lipase PS was 50 °C.

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Nanobioconjugates of Candida antarctica lipase B and single-walled carbon nanotubes in biodiesel production

Cited by 71 publications

References 33 publications

Lipase based static emulsions as efficient biocatalysts for biodiesel production

Lipase based static emulsions as efficient biocatalysts for biodiesel production

Efficient Biodiesel Production Catalyzed by Nanobioconjugate of Lipase from Pseudomonas fluorescens

Bisepoxide-activated Hollow Silica Microspheres for Covalent Immobilization of Lipase from Burkholderia cepacia

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