Liquid lipase preparations designed for industrial production of biodiesel. Is it really an optimal solution?

Monteiro, Rodolpho R. C.; Arana-Peña, Sara; Rocha, Thays N. da; Miranda, Letícia Passos; Berenguer-Murcia, Ángel; Tardioli, Paulo Waldir; Santos, José Cleiton Sousa dos; Fernández‐Lafuente, Roberto

doi:10.1016/j.renene.2020.10.071

Cited by 104 publications

(55 citation statements)

References 351 publications

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“…Eversa-mCLEA was less active using short-chain primary alcohols (methanol and ethanol), which are the alcohols usually utilized in biodiesel production [ 67 , 68 , 69 ]. This lower activity can be explained by the fact of methanol and ethanol change the hydration layer of the enzyme [ 21 , 70 , 71 , 72 ], justifying the common practice of adding the alcohol in steps, mainly when methanol is used as an acyl acceptor ([ 24 ]). Similar results were obtained by Trivedi et al [ 66 ] using the formulation preceding Eversa (soluble lipase Callera Trans L, EP 258068) in the esterification reaction of short and long-chain primary alcohols (oleyl alcohol, octanol, and hexanol), for which the ester yield reduced as the length of the chain decreased.…”

Section: Resultsmentioning

confidence: 99%

“…Up to date, Eversa has been mainly utilized for biodiesel production using oils and fats and short-chain alcohols [ 26 , 74 , 75 ]; there is no evidence of its use in the synthesis of biolubricants [ 24 ]. This may be due to the poor performance of liquid Eversa in this reaction.…”

Section: Resultsmentioning

confidence: 99%

“…Eversa ® Transform 2.0 was initially launched to be used as a liquid biocatalyst in the production of biodiesel [ 23 , 24 ]. However, it has been shown that if the enzyme is properly immobilized, the enzyme performance could be improved in diverse applications, such as biodiesel [ 25 , 26 , 27 ], free fatty acid (FFA) [ 28 ], or glyceride [ 29 ] production, among others process [ 24 ]. Eversa is a genetically modified industrial evolution of the lipase from Thermomyces lanuginosus (TLL) expressed in Aspergillus oryzae by Novozymes A/S [ 24 , 30 ].…”

Section: Introductionmentioning

confidence: 99%

“…However, it has been shown that if the enzyme is properly immobilized, the enzyme performance could be improved in diverse applications, such as biodiesel [ 25 , 26 , 27 ], free fatty acid (FFA) [ 28 ], or glyceride [ 29 ] production, among others process [ 24 ]. Eversa is a genetically modified industrial evolution of the lipase from Thermomyces lanuginosus (TLL) expressed in Aspergillus oryzae by Novozymes A/S [ 24 , 30 ]. Although both enzymes are similar in terms of primary sequence, a recent comparison between them showed that the functional properties could be fairly different [ 31 ].…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of Eversa® Transform via CLEA Technology Converts It in a Suitable Biocatalyst for Biolubricant Production Using Waste Cooking Oil

et al. 2021

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The performance of the previously optimized magnetic cross-linked enzyme aggregate of Eversa (Eversa-mCLEA) in the enzymatic synthesis of biolubricants by transesterification of waste cooking oil (WCO) with different alcohols has been evaluated. Eversa-mCLEA showed good activities using these alcohols, reaching a transesterification activity with isoamyl alcohol around 10-fold higher than with methanol. Yields of isoamyl fatty acid ester synthesis were similar using WCO or refined oil, confirming that this biocatalyst could be utilized to transform this residue into a valuable product. The effects of WCO/isoamyl alcohol molar ratio and enzyme load on the synthesis of biolubricant were also investigated. A maximum yield of around 90 wt.% was reached after 72 h of reaction using an enzyme load of 12 esterification units/g oil and a WCO/alcohol molar ratio of 1:6 in a solvent-free system. At the same conditions, the liquid Eversa yielded a maximum ester yield of only 34%. This study demonstrated the great changes in the enzyme properties that can be derived from a proper immobilization system. Moreover, it also shows the potential of WCO as a feedstock for the production of isoamyl fatty acid esters, which are potential candidates as biolubricants.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Immobilization of Eversa® Transform via CLEA Technology Converts It in a Suitable Biocatalyst for Biolubricant Production Using Waste Cooking Oil

et al. 2021

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“…As lipases, this study includes the lipases A and B from Candida antarctica (CALA and CALB) [ 82 , 83 , 84 , 85 , 86 , 87 , 88 ], and the lipases from Candida rugosa (CRL) [ 89 ] and from Rhizomucor miehei (RML) [ 90 , 91 ]. Moreover, Eversa ® Transform 2.0 (EVT), a recombinant commercial enzyme that has been improved from the initial lipase from Thermomyces lanuginosus to improve their performance in biodiesel production [ 92 , 93 ] has been also studied. The proteases ficin from Ficus carica [ 94 , 95 ], chymotrypsin from bovine liver [ 96 , 97 ] and trypsin from bovine liver [ 98 , 99 ] have been immobilized on glyoxyl agarose [ 100 , 101 ] and glutaraldehyde-amino agarose beads [ 102 ].…”

Section: Introductionmentioning

confidence: 99%

Effect of Concentrated Salts Solutions on the Stability of Immobilized Enzymes: Influence of Inactivation Conditions and Immobilization Protocol

et al. 2021

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This paper aims to investigate the effects of some salts (NaCl, (NH4)2SO4 and Na2SO4) at pH 5.0, 7.0 and 9.0 on the stability of 13 different immobilized enzymes: five lipases, three proteases, two glycosidases, and one laccase, penicillin G acylase and catalase. The enzymes were immobilized to prevent their aggregation. Lipases were immobilized via interfacial activation on octyl agarose or on glutaraldehyde-amino agarose beads, proteases on glyoxyl agarose or glutaraldehyde-amino agarose beads. The use of high concentrations of salts usually has some effects on enzyme stability, but the intensity and nature of these effects depends on the inactivation pH, nature and concentration of the salt, enzyme and immobilization protocol. The same salt can be a stabilizing or a destabilizing agent for a specific enzyme depending on its concentration, inactivation pH and immobilization protocol. Using lipases, (NH4)2SO4 generally permits the highest stabilities (although this is not a universal rule), but using the other enzymes this salt is in many instances a destabilizing agent. At pH 9.0, it is more likely to find a salt destabilizing effect than at pH 7.0. Results confirm the difficulty of foreseeing the effect of high concentrations of salts in a specific immobilized enzyme.

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Transesterification of waste cooking oil with a commercial liquid biocatalyst: Key information revised and new insights

Mateos

Casella

Briand

et al. 2023

J Americ Oil Chem Soc

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The transesterification of the waste cooking oil (WCO) with various linear alcohols (C1 to C4) using the commercial biocatalyst Eversa ® Transform in its liquid form is addressed in this investigation. The influence of the amount of the liquid formulation of lipase Eversa ® Transform, nature of alcohol, oil to alcohol molar ratio and water addition in the transesterification of fresh sunflower oil and WCO was investigated. In addition, an innovative combination of that fungal based biocatalyst with a native vegetable lipase, known as Araujia sericifera (ASL), in a liquid formulation fashion was investigated. The assays carried out at 35 C for 24 h, an oil: alcohol molar ratio of 1:6.8, 2% v/w water added and 1% v/w of biocatalyst allowed to obtain up to 90% conversion and yield towards fatty acid methyl, ethyl and propyl esters. In the particular case of 1-butanol (C4) a 79% conversion and 72% yield to the esters was obtained. The biocatalyst maintains about 60% of its activity in the conversion of glycerides and yield towards the esters. The combination of process using Eversa ® Transform and then the ASL lipase in the transesterification of the WCO probed efficient in the conversion of triglycerides using 1-butanol. A shift from 73 wt % of fatty acid butyl esters (FABE) towards 90 wt % was achieved.

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Liquid lipase preparations designed for industrial production of biodiesel. Is it really an optimal solution?

Cited by 104 publications

References 351 publications

Immobilization of Eversa® Transform via CLEA Technology Converts It in a Suitable Biocatalyst for Biolubricant Production Using Waste Cooking Oil

Immobilization of Eversa® Transform via CLEA Technology Converts It in a Suitable Biocatalyst for Biolubricant Production Using Waste Cooking Oil

Effect of Concentrated Salts Solutions on the Stability of Immobilized Enzymes: Influence of Inactivation Conditions and Immobilization Protocol

Transesterification of waste cooking oil with a commercial liquid biocatalyst: Key information revised and new insights

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