Biodiesel production catalysed by low-cost liquid enzyme Eversa® Transform 2.0: Effect of free fatty acid content on lipase methanol tolerance and kinetic model

Chang, Mun Yuen; Chan, Eng Seng; Song, Cher Pin

doi:10.1016/j.fuel.2020.119266

Cited by 88 publications

(32 citation statements)

References 34 publications

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“…In the research of the Eversa Transform 2.0 immobilized on Seapabeads-C18 was using for the transesteri cation of sun ower oil in an anhydrous medium using hexane as a solvent, the performance of the immobilized enzyme in a higher molar ratio of methanol 12:1 (M:O) was better resulting in yield 80 wt% FAME, the solvent absence affects the excellent performance this immobilized lipase. Chang [11] investigated the methanol tolerance of liquid lipase Eversa Transform 2. According to with study the enhanced methanol tolerance of the enzyme may be attributed to the gentler environment created by the water.…”

Section: Effect Of Molar Ratio Alcohol In the Transesteri Cation Of Sun Ower Oil Catalyzed By Sepabeads-eversa Lipasesmentioning

confidence: 99%

“…Most of the published studies about Eversa lipases are transesteri cation of triglycerides or esteri cation of free fatty acids and used these enzymes in the free form [8][9][10][11][12]. Even though Eversa enzymes may be used in free form, their immobilization may enhance many properties such as stability and resistance to inhibitors chemicals [13].…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of Eversa Lipases on Hydrophobic Supports for Production of Oleate Esters Solvent-Free

Fernández‐Lorente

Remonatto

Oliveira

et al. 2021

Preprint

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Lipases are an important group of biocatalysts for many industrial applications. Two new commercial low-cost lipases Eversa® Transform and Eversa® Transform 2.0 was immobilized on four different hydrophobic supports: Lewatit-DVB, Purolite-DVB, Sepabeads-C18, and Purolite-C18. The performance of immobilized lipases was investigated in the transesterification of sunflower oil solvent-free in an anhydrous medium. Interesting results were obtained for both lipases and the four supports, but with Sepabeads support the lipases Eversa showed high catalytic activity. However, the more stable and efficient derivative was Eversa® Transform immobilized on Sepabeads C-18. A 98 wt% of ethyl ester of fatty acid (FAEE) was obtained, in 3 hours at 40ºC, ethanol/sunflower oil molar ratio of 3:1 and a 10 wt% of the immobilized biocatalyst. After 6 reaction cycles, the immobilized biocatalyst preserved 70 wt% of activity. Both lipases immobilized in Sepabeads C-18 were highly active and stable in the presence of ethanol. The immobilization of Eversa Transform and Eversa Transform 2.0 in hydrophobic supports described in this study appears to be a promising alternative to the immobilization and application of these news lipases still unexplored.

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Section: Effect Of Molar Ratio Alcohol In the Transesteri Cation Of Sun Ower Oil Catalyzed By Sepabeads-eversa Lipasesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Immobilization of Eversa Lipases on Hydrophobic Supports for Production of Oleate Esters Solvent-Free

Fernández‐Lorente

Remonatto

Oliveira

et al. 2021

Preprint

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“…In 2015, Novozymes released a new enzyme, Eversa Transform 2.0 27 . This enzyme, as far as we are aware, has only been tested by Chang et al 28 . and Sun et al 29 .…”

Section: Introductionmentioning

confidence: 99%

“…for the production of biodiesel from refined palm oil and Semen Abutili seed oil respectively. Chang et al 28 . carried out a reaction with a methanol oil molar ratio of 8:1, at a reaction temperature of 40 °C for 24 h, achieving a 97% yield.…”

Section: Introductionmentioning

confidence: 99%

Optimization of the enzymatic butanolysis of jatropha oil for biodiesel production using Eversa

Acherki

Bouaid

Marchetti

2021

Biofuels Bioprod Bioref

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The use of non‐edible oils for energy production is attracting increasing attention, with a particular focus on those oils that can be produced from plants growing in non‐arable areas. Among the possible alternatives, oils with high free fatty acid content, such as jatropha, have shown great potential. The optimization of jatropha oil in the presence of a bio‐based alcohol (butanol) was investigated for the production of biodiesel using a commercial enzyme (Eversa from Novozymes). The optimization was conducted by changing the reaction temperature and the amount of catalyst, with a 6:1 butanol/oil molar ratio, while the reaction time was set to 60 min. The optimal result was found at the highest reaction temperature (42 °C) and the highest catalyst amount (9.79%), with a biodiesel yield of 83%. A second optimization was conducted, allowing the time to run for up to 8 h. Here the final biodiesel produced was in line with the EU14214 standards, fulfilling all the requirements with the exception of the requirement for oxidation stability. In addition to fulfilling most of the EU14214 standards, the cost of this new enzyme is lower than that of other commercial alternatives. Results show that biodiesel produced using butanol as alcohol in the transesterification process improved cold flow properties in terms of cloud point (CP), pour point (PP), and cold filter plugging point (CFPP). © 2021 The Authors. Biofuels, Bioproducts and Biorefining published by Society of Industrial Chemistry and John Wiley & Sons Ltd.

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“…Many free and immobilized microbial lipases have been tested as catalysts of the synthesis of biodiesel [9]. In the last years, enzymes like Candida antarctica lipase A (Cal A) [37] and very specially Eversa Transform ® , a genetically-modified variant of the lipase from Thermomyces lanuginosus designed by Novozymes for the synthesis of biodiesel, have been used in this application [36,[38][39][40][41][42]. Both biocatalysts have been immobilized by hydrophobicity on octyl agarose beads [24,39,43], Cal A was also covalently attached to chitosan-coated magnetic nanoparticles activated with GA [44], and mCLEAs of Eversa Transform ® were prepared and tested to produce biodiesel [41].…”

Section: Introductionmentioning

confidence: 99%

Immobilized Forms of the Ophiostoma piceae Lipase for Green Synthesis of Biodiesel. Comparison with Eversa Transform 2.0 and Cal A

Molina-Gutiérrez

Alcaraz

López

et al. 2021

JoF

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In this work, we analyzed the suitability of a versatile recombinant lipase, secreted by Ophiostoma piceae (OPEr) and produced in Pichia pastoris, as a catalyst of the synthesis of biodiesel. The enzyme was immobilized by five covalent procedures and by hydrophobicity on functionalized nanoparticles of magnetite or of a novel Zn/Mn oxide named G1. Then, they were tested for green production of biodiesel by solventless enzymatic transesterification of discarded cooking oil and methanol (1:4) at 25 °C. The results were compared with those shown by free OPEr and the commercial lipases Eversa® and Cal A®. Several preparations with immobilized OPEr produced high synthesis yields (>90% transesterification), comparable to those obtained with Eversa®, the commercial enzyme designed for this application. Three of the biocatalysts maintained their catalytic efficiency for nine cycles. The process catalyzed by AMNP-CH-OPEr was scaled from 500 µL to 25 mL (50 times), improving its efficiency.

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Biodiesel production catalysed by low-cost liquid enzyme Eversa® Transform 2.0: Effect of free fatty acid content on lipase methanol tolerance and kinetic model

Cited by 88 publications

References 34 publications

Immobilization of Eversa Lipases on Hydrophobic Supports for Production of Oleate Esters Solvent-Free

Immobilization of Eversa Lipases on Hydrophobic Supports for Production of Oleate Esters Solvent-Free

Optimization of the enzymatic butanolysis of jatropha oil for biodiesel production using Eversa

Immobilized Forms of the Ophiostoma piceae Lipase for Green Synthesis of Biodiesel. Comparison with Eversa Transform 2.0 and Cal A

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