Improved stability of immobilized lipases via modification with polyethylenimine and glutaraldehyde

Zaak, Hadjer; Fernández-López, Laura; Otero, Cristina; Sassi, Mohamed; Fernández‐Lafuente, Roberto

doi:10.1016/j.enzmictec.2017.07.001

Cited by 72 publications

(45 citation statements)

References 78 publications

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“…The solvent inactivation of octyl lipase preparations is associated to the enzyme release from the support [53][54][55][56][60][61][62]] and this will not occur in MANAE. Apparently, Eversa became so strongly adsorbed on octyl agarose that this effect was not very significant.…”

Section: Inactivation Of the Enzyme Preparations In Organic Solventsmentioning

confidence: 99%

“…Apparently, Eversa became so strongly adsorbed on octyl agarose that this effect was not very significant. Furthermore, the coating of the enzymes with PEI has prevented enzyme leakage and the promotion of a certain solvent partition as main functions [60][61][62]. Using octyl-Eversa, only using dioxane the effect is somehow positive, with acetonitrile and methanol the PEI coating effect is even negative.…”

Section: Inactivation Of the Enzyme Preparations In Organic Solventsmentioning

confidence: 99%

“…Another simpler alternative is the chemical or physical crosslinking of the enzyme molecules, which reduces the risks of enzyme release from the support [59]. The coating of immobilized lipases with PEI is one of the most used proposals [60][61][62], as this reagent may have many positive impacts in enzyme properties. [63].…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features

2018

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Eversa is an enzyme recently launched by Novozymes to be used in a free form as biocatalyst in biodiesel production. This paper shows for first time the immobilization of Eversa (a commercial lipase) on octyl and aminated agarose beads and the comparison of the enzyme properties to those of the most used lipase, the isoform B from Candida antarctica (CALB) immobilized on octyl agarose beads. Immobilization on octyl and aminated supports of Eversa has not had a significant effect on enzyme activity versus p-nitrophenyl butyrate (pNPB) under standard conditions (pH 7), but immobilization on octyl agarose beads greatly enhanced the stability of the enzyme under all studied conditions, much more than immobilization on aminated support. Octyl-Eversa was much more stable than octyl-CALB at pH 9, but it was less stable at pH 5. In the presence of 90% acetonitrile or dioxane, octyl-Eversa maintained the activity (even increased the activity) after 45 days of incubation in a similar way to octyl-CALB, but in 90% of methanol, results are much worse, and octyl-CALB became much more stable than Eversa. Coating with PEI has not a clear effect on octyl-Eversa stability, although it affected enzyme specificity and activity response to the changes in the pH. Eversa immobilized octyl supports was more active than CALB versus triacetin or pNPB, but much less active versus methyl mandelate esters. On the other hand, Eversa specificity and response to changes in the medium were greatly modulated by the immobilization protocol or by the coating of the immobilized enzyme with PEI. Thus, Eversa may be a promising biocatalyst for many processes different to the biodiesel production and its properties may be greatly improved following a suitable immobilization protocol, and in some cases is more stable and active than CALB.

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Section: Inactivation Of the Enzyme Preparations In Organic Solventsmentioning

confidence: 99%

Section: Inactivation Of the Enzyme Preparations In Organic Solventsmentioning

confidence: 99%

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Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features

2018

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“…Compared with free enzymes, there are several advantages for using immobilized enzymes, which include their stability of conformation, easy separation, and reusability . As shown in Figure , the e.e .…”

Section: Resultsmentioning

confidence: 99%

The enzymatic resolution of 1‐(4‐chlorophenyl)ethylamine by Novozym 435 to prepare a novel triazolopyrimidine herbicide

et al. 2018

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The kinetic resolution of (R,S)‐1‐(4‐chlorophenyl)ethylamine was accomplished using a commercial lipase from Candida antarctica (Novozym 435). The performance of this lipase was investigated for the enantioselective amidation of (R,S)‐1‐(4‐chlorophenyl)ethylamine, leaving the target product (S)‐1‐(4‐chlorophenyl)ethylamine in its unreacted form. The effects of various types of solvents and an acyl donor, the molar ratio of the substrate to the acyl donor, and the reaction temperature were studied. The optimum reaction conditions were found to result in amidation with methyl 2‐tetrahydrofuroate at 40°C in methyl tert‐butyl ether, with a substrate/acyl donor molar ratio of 1:2.4. The conversion rate of (R,S)‐1‐(4‐chlorophenyl)ethylamine was 52%, with an enantiomeric excess of 99% towards the unreacted substrate in a reaction time of 22 hours. Finally, using optically pure (S)‐1‐(4‐chlorophenyl)ethylamine as the raw material, the chemical synthesis of (S)‐N‐(1‐(4‐chlorphenyl)ethyl)‐2‐(5,7‐dimethyl‐[1,2,4]triazolo[1,5‐a]pyrimidin‐2‐ylthio)acetamide, a novel triazolopyrimidine herbicide, was achieved, and the total yield and purity were 83.5% and 95.3%, respectively.

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“…Anyhow, the inherent drawback of this immobilization protocol is caused by the enzyme release from the carrier to the medium, under certain conditions and in the presence of detergent-like molecules [311], reducing the range of reaction conditions where these biocatalysts may be used ( Figure 20). This has been solved using different heterofunctional supports, bearing different groups on the support surface with different functions for a better control of the immobilization procedure [312][313][314][315], performing the physical intermolecular crosslinking of the immobilized enzyme using polyethylenimine [316][317][318] or using dexOx as chemical crosslinking reagent [319] ( Figure 21). The large size and number of functional groups of dexOx allow multi-intermolecular enzyme crosslinking, thus preventing enzyme release.…”

Section: -Use Of Dexox For Intermolecular Crosslinking Of Immobilizedmentioning

confidence: 99%

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

et al. 2019

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Dextran aldehyde (dexOx), resulting from the periodate oxidative cleavage of 1,2-diol moiety inside dextran, is a polymer that is very useful in many areas, including as a macromolecular carrier for drug delivery and other biomedical applications. In particular, it has been widely used for chemical engineering of enzymes, with the aim of designing better biocatalysts that possess improved catalytic properties, making them more stable and/or active for different catalytic reactions. This polymer possesses a very flexible hydrophilic structure, which becomes inert after chemical reduction; therefore, dexOx comes to be highly versatile in a biocatalyst design. This paper presents an overview of the multiple applications of dexOx in applied biocatalysis, e.g., to modulate the adsorption of biomolecules on carrier surfaces in affinity chromatography and biosensors design, to serve as a spacer arm between a ligand and the support in biomacromolecule immobilization procedures or to generate artificial microenvironments around the enzyme molecules or to stabilize multimeric enzymes by intersubunit crosslinking, among many other applications.

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Improved stability of immobilized lipases via modification with polyethylenimine and glutaraldehyde

Cited by 72 publications

References 78 publications

Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features

Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features

The enzymatic resolution of 1‐(4‐chlorophenyl)ethylamine by Novozym 435 to prepare a novel triazolopyrimidine herbicide

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

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