Coimmobilization of different lipases: Simple layer by layer enzyme spatial ordering

Arana-Peña, Sara; Rios, Nathália Saraiva; Mendez-Sanchez, Carmen; Lokha, Yuliya; Carballares, Diego; Gonçalves, Leandra Regina; Fernández‐Lafuente, Roberto

doi:10.1016/j.ijbiomac.2019.10.087

Cited by 41 publications

(37 citation statements)

References 67 publications

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“…The coating of this three-component co-immobilized combilipase with PEI has also diverse effects depending on the substrate, in agreement with previous positive effects reported of this treatment for the activity of these immobilized enzymes in octyl agarose [91][92][93]. PEI modification of many immobilized enzymes is a usual tool to improve enzyme performance, as stated in the introduction [83].…”

Section: Building Of the Combilipasessupporting

confidence: 86%

“…Some hyperactivation upon immobilization (by 2.5 folds using LEU, by 5 using RML) was observed. These positive effects on enzyme activity remained with a similar intensity after 24 h. These results could be related to the positive effects that the coating with PEI presented when used to coat immobilized LEU or RML [92,93,104]. Next, we checked the stability of the PEI-immobilized enzymes.…”

Section: Immobilization and Stability Of Leu And Rml In A Support Coamentioning

confidence: 66%

“…Moreover, it may prevent enzyme release of the just physically adsorbed lipase molecules [86,90]. Finally, it has been successfully employed as an adhesive agent in the production of lipase multilayers [91][92][93].…”

Section: Introductionmentioning

confidence: 99%

“…In this paper, we have used different lipases to prepare a multi (five lipase component)-co-immobilized biocatalyst using octyl-vinyl sulfone agarose as immobilization support [94] and PEI as adhesive agent between the two enzyme layers (the ones in contact with the support surface, that will be the most stable enzymes, and the ones in contact with the polymer, that will be the least stable enzymes) [82,[91][92][93]. Octyl-vinyl sulfone (octyl-VS) has been used to prevent enzyme release from the support under any kind of operation conditions.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Building Of the Combilipasessupporting

confidence: 86%

Section: Immobilization and Stability Of Leu And Rml In A Support Coamentioning

confidence: 66%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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“…In fact, it has been proposed to coat Novozym 435 with PEI with some positive results in the biodiesel production process by these biocatalyst [103,104]. Moreover, this treatment, in some instances, has increased lipase activity [93,[105][106][107]. However, in this case, this treatment promoted a slight decrease in the activity of both immobilized biocatalysts.…”

Section: Effect Of the Modification With Pei On The Activities Of Thementioning

confidence: 99%

Immobilized Biocatalysts of Eversa® Transform 2.0 and Lipase from Thermomyces Lanuginosus: Comparison of Some Properties and Performance in Biodiesel Production

et al. 2020

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Eversa® Transform (ET), and the lipase from Thermomyces lanuginosus (TLL), liquid commercial lipases formulations, have been immobilized on octyl agarose beads and their stabilities were compared. Immobilized and free ET forms were more thermostable than TLL formulations at pH 5.0, 7.0, and 9.0, and the ET immobilized form was more stable in the presence of 90% methanol or dioxane at 25 °C and pH 7. Specific activity versus p-nitrophenyl butyrate was higher for ET than for TLL. However, after immobilization the differences almost disappeared because TLL was very hyperactivated (2.5-fold) and ET increased the activity only by 1.6 times. The enzymes were also immobilized in octadecyl methacrylate beads. In both cases, the loading was around 20 mg/g. In this instance, activity was similar for immobilized TLL and ET using triacetin, while the activity of immobilized ET was lower using (S)-methyl mandelate. When the immobilized enzymes were used to produce biodiesel from sunflower oil and methanol in tert-butanol medium, their performance was fairly similar.

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Waste Derived Supports for Immobilization of Lipase Towards Enhancing Efficiency and Reusability of Enzymes

Mitra

Kamila

Ghodke

et al. 2022

Clean Energy Production Technologies

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Coimmobilization of different lipases: Simple layer by layer enzyme spatial ordering

Cited by 41 publications

References 67 publications

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

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

Immobilized Biocatalysts of Eversa® Transform 2.0 and Lipase from Thermomyces Lanuginosus: Comparison of Some Properties and Performance in Biodiesel Production

Waste Derived Supports for Immobilization of Lipase Towards Enhancing Efficiency and Reusability of Enzymes

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