Effects of a combination of lipases immobilised on desilicated and thiol-modified ZSM-5 for the synthesis of ethyl esters from macauba pulp oil in a solvent-free system

Araki, Carina Akemi; Marcucci, Sílvio Miguel Parmegiani; Silva, Lidiane Sabino da; Maeda, Celso Hissao; Arroyo, Pedro Augusto; Zanin, Gisella Maria

doi:10.1016/j.apcata.2018.06.007

Cited by 22 publications

(15 citation statements)

References 36 publications

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“…However, these features become a problem when the biocatalyst is going to be utilized in the full modification of a heterogeneous substrate. This is the case of oils, either when they are hydrolyzed to produce free fatty acids or when they are used in transesterifications to produce biodiesel [16][17][18][19][20][21][22][23]. It should be considered that the oil will be composed of many different triglycerides formed by different fatty acids.…”

Section: Introductionmentioning

confidence: 99%

“…Thus, it is not easy to find an "optimal" enzyme that may be the best one in all situations. In these cases, it has been shown that the combined use of several lipases permits not only better yields but also higher initial reaction rates and more lineal reaction courses (in some cases one enzyme eliminates an inhibitor of the main enzyme) [16][17][18][19][20][21][22][23]. Usually, this has been obtained using mixtures of individually immobilized lipases [16][17][18][19][20][21][22][23].…”

Section: Introductionmentioning

confidence: 99%

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Reuse of Lipase from Pseudomonas fluorescens via Its Step-by-Step Coimmobilization on Glyoxyl-Octyl Agarose Beads with Least Stable Lipases

et al. 2019

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Coimmobilization of lipases may be interesting in many uses, but this means that the stability of the least stable enzyme determines the stability of the full combilipase. Here, we propose a strategy that permits the reuse the most stable enzyme. Lecitase Ultra (LU) (a phospholipase) and the lipases from Rhizomucor miehei (RML) and from Pseudomonas fluorescens (PFL) were immobilized on octyl agarose, and their stabilities were studied under a broad range of conditions. Immobilized PFL was found to be the most stable enzyme under all condition ranges studied. Furthermore, in many cases it maintained full activity, while the other enzymes lost more than 50% of their initial activity. To coimmobilize these enzymes without discarding fully active PFL when LU or RML had been inactivated, PFL was covalently immobilized on glyoxyl-agarose beads. After biocatalysts reduction, the other enzyme was coimmobilized just by interfacial activation. After checking that glyoxyl-octyl-PFL was stable in 4% Triton X-100, the biocatalysts of PFL coimmobilized with LU or RML were submitted to inactivation under different conditions. Then, the inactivated least stable coimmobilized enzyme was desorbed (using 4% detergent) and a new enzyme reloading (using in some instances RML and in some others employing LU) was performed. The initial activity of immobilized PFL was maintained intact for several of these cycles. This shows the great potential of this lipase coimmobilization strategy.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Reuse of Lipase from Pseudomonas fluorescens via Its Step-by-Step Coimmobilization on Glyoxyl-Octyl Agarose Beads with Least Stable Lipases

et al. 2019

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“…Under these circumstances, it is highly unlikely that an individual lipase may be the optimal one for the full transformation of these heterogeneous substrates. That way, it has been shown that the combined use of different lipases, combining different enzyme specificities, selectivities or different sensibility to changes in the reaction conditions, produces a faster reaction and a higher conversion yield, mainly when using these heterofunctional substrates [43][44][45][46][47][48][49][50][51][52][53][54][55][56]. Even the use of the same lipase immobilized following different strategies may permit to get this positive effect [57].…”

Section: Introductionmentioning

confidence: 99%

Multi-Combilipases: Co-Immobilizing Lipases with Very Different Stabilities Combining Immobilization via Interfacial Activation and Ion Exchange. The Reuse of the Most Stable Co-Immobilized Enzymes after Inactivation of the Least Stable Ones

et al. 2020

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The lipases A and B from Candida antarctica (CALA and CALB), Thermomyces lanuginosus (TLL) or Rhizomucor miehei (RML), and the commercial and artificial phospholipase Lecitase ultra (LEU) may be co-immobilized on octyl agarose beads. However, LEU and RML became almost fully inactivated under conditions where CALA, CALB and TLL retained full activity. This means that, to have a five components co-immobilized combi-lipase, we should discard 3 fully active and immobilized enzymes when the other two enzymes are inactivated. To solve this situation, CALA, CALB and TLL have been co-immobilized on octyl-vinyl sulfone agarose beads, coated with polyethylenimine (PEI) and the least stable enzymes, RML and LEU have been co-immobilized over these immobilized enzymes. The coating with PEI is even favorable for the activity of the immobilized enzymes. It was checked that RML and LEU could be released from the enzyme-PEI coated biocatalyst, although this also produced some release of the PEI. That way, a protocol was developed to co-immobilize the five enzymes, in a way that the most stable could be reused after the inactivation of the least stable ones. After RML and LEU inactivation, the combi-biocatalysts were incubated in 0.5 M of ammonium sulfate to release the inactivated enzymes, incubated again with PEI and a new RML and LEU batch could be immobilized, maintaining the activity of the three most stable enzymes for at least five cycles of incubation at pH 7.0 and 60 °C for 3 h, incubation on ammonium sulfate, incubation in PEI and co-immobilization of new enzymes. The effect of the order of co-immobilization of the different enzymes on the co-immobilized biocatalyst activity was also investigated using different substrates, finding that when the most active enzyme versus one substrate was immobilized first (nearer to the surface of the particle), the activity was higher than when this enzyme was co-immobilized last (nearer to the particle core).

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“…No entanto, o uso das enzimas imobilizadas em suportes sólidos promove maior estabilidade física e térmica, facilita sua remoção do meio reacional e permite serem reutilizadas em um novo ciclo, favorecendo redução nos custos global do processo. Além disso, o uso de combinações enzimáticas possibilita cinética reacional mais rápida e a redução do teor de MAG e DAG do produto formado (POPPE et al, 2013;ARAKI et al, 2018;POPPE et al, 2015).…”

Section: Introductionunclassified

“…, para o óleo de palma a associação das lipases TLL e RML foi mais efetiva fornecendo 80% de conversão em 18 horas de reação.A atuação sinérgica de enzimas com diferentes especificidades na produção de ésteres etílicos também foi relatada porAraki et al (2018). As lipases imobilizadas de Burkholderia cepacia e Thermomyces lanuginosus combinadas na proporção de 50% cada, proporcionou conversão de 77% do óleo de macaúba em 48 h de reação, enquanto as reações utilizando isoladamente as lipases de B. cepacia e T. lanuginosus, forneceram conversões de 40 e 53%, Imobilização da lipase A imobilização das lipases aplicadas ao processo de produção de biodiesel tem como uma das finalidades torná-las insolúveis ao meio reacional, facilitando sua remoção e permitindo reutilização.…”

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Produção de biodiesel a partir do óleo de palmiste: aplicação de combi-lipases como biocatalisadores em reatores descontínuo e contínuo

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Effects of a combination of lipases immobilised on desilicated and thiol-modified ZSM-5 for the synthesis of ethyl esters from macauba pulp oil in a solvent-free system

Cited by 22 publications

References 36 publications

Reuse of Lipase from Pseudomonas fluorescens via Its Step-by-Step Coimmobilization on Glyoxyl-Octyl Agarose Beads with Least Stable Lipases

Reuse of Lipase from Pseudomonas fluorescens via Its Step-by-Step Coimmobilization on Glyoxyl-Octyl Agarose Beads with Least Stable Lipases

Multi-Combilipases: Co-Immobilizing Lipases with Very Different Stabilities Combining Immobilization via Interfacial Activation and Ion Exchange. The Reuse of the Most Stable Co-Immobilized Enzymes after Inactivation of the Least Stable Ones

Produção de biodiesel a partir do óleo de palmiste: aplicação de combi-lipases como biocatalisadores em reatores descontínuo e contínuo

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