Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2

Fernández-López, Laura; Rueda, Nazzoly; Bartolome-Cabrero, Rocio; Rodríguez, María Gabriela Lagos; Albuquerque, Tiago Lima de; Santos, José Cleiton Sousa dos; Barbosa, Oveimar; Fernández-Lafuente, Roberto

doi:10.1016/j.procbio.2015.11.015

Cited by 67 publications

(25 citation statements)

References 22 publications

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“…The multivalent covalent attachment of enzymes to activated substrates is considered a very important tool for stabilizing proteins. [53][54][55][56][57][58][59][60] The number of chemical bonds between support and enzyme is what defines the stabilization factor of the immobilized enzyme. 53,54 The formation of multiple chemical covalent bonds is one that maintains the relative positions of all chemical groups involved in the immobilization unaltered during the conformational change induced by any distorted agent (organic solvents, heat, and extreme pH values).…”

Section: Multipoint Covalent Attachmentmentioning

confidence: 99%

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Reis

Sousa

Serpa

et al. 2019

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The enzymatic processes are increasingly highlights, especially in the synthesis of chemical products with high added value. The enzyme immobilization can improve industrial biocatalytic processes. The immobilization of enzymes provides the production of efficient, stable biocatalysts, possibility of reuse and easy purification of the products, when compared to the free enzymes. There is a growing research for more efficient methods of enzyme immobilization. In this context, the choice of support and immobilization strategy can significantly improve the final enzymatic properties. In this review paper, we aimed to discuss the versatility of biocatalysts immobilized enzymes design, focusing on the opportunities and disadvantages for each method presented. They discussed the recent development of enzyme immobilization methods and applications relating the final properties of the produced biocatalysts with the desired goals.

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Section: Multipoint Covalent Attachmentmentioning

confidence: 99%

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Reis

Sousa

Serpa

et al. 2019

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“…However, these effects were only on stability at high temperature or very high buffer concentration, the activity remained unaltered when changing the buffer [75]. On the other hand, some cations (e.g., Ca 2+ ) have shown to have positive effects on some lipase stabilities [76,77]. Curiously, this effect depends on the pH and immobilization lipase form [76,77].…”

Section: Effect Of Some Ions On the Lipase Stabilitymentioning

confidence: 99%

“…the other hand, some cations (e.g., Ca 2+ ) have shown to have positive effects on some lipase stabilities [76,77]. Curiously, this effect depends on the pH and immobilization lipase form [76,77]. Thus, we have decided to analyze the effect of CaCl2 and sodium phosphate on the stability of the different Eversa forms at pH 7, compared to octyl-CALB.…”

Section: Effect Of Some Ions On the Lipase Stabilitymentioning

confidence: 99%

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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“…According to recent studies, we can see that covalent binding methods were first selected to immobilize lipase. Because of its ability to rigidify the location of the immobilized enzyme, improved selectivity and stability can be achieved via covalent bonding, however, the most critical point is that the spatial structure of protein can be changed by covalent attachment, leading to damage to the enzyme activity center, thereby reducing the enzyme activity [ 14 , 15 , 24 , 25 , 26 , 27 ]. Moreover, it is well known that physical adsorption-immobilization via intermolecular interaction, preserves well the structures of both the nanomaterial and the protein, and maximizes the catalytic performance of enzymes.…”

Section: Introductionmentioning

confidence: 99%

Preparation of Carriers Based on ZnO Nanoparticles Decorated on Graphene Oxide (GO) Nanosheets for Efficient Immobilization of Lipase from Candida rugosa

et al. 2017

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Herein, a promising carrier, graphene oxide (GO) decorated with ZnO nanoparticles, denoted as GO/ZnO composite, has been designed and constructed. This carrier was characterized by X-ray powder diffraction, scanning electron microscopy, Fourier transform infrared spectroscopy and thermogravimetry. Then, Candida rugosa lipase (CRL) was immobilized onto the GO-based materials via physical adsorption. Our results indicated that the lipase loading amount on the GO/ZnO composites was about 73.52 mg of protein per g. In the activity assay, the novel immobilized lipase GO/ZnO@CRL, exhibited particularly excellent performance in terms of thermostability and reusability. Within 30 min at 50 °C, the free lipase, GO@CRL and ZnO@CRL had respectively lost 64%, 62% and 41% of their initial activity. However, GO/ZnO@CRL still retained its activity of 63% after 180 min at 50 °C. After reuse of the GO/ZnO@CRL 14 times, 90% of the initial activity can be recovered. Meanwhile, the relative activity of GO@CRL and ZnO@CRL was 28% and 23% under uniform conditions. Hence, GO-decorated ZnO nanoparticles may possess great potential as carriers for immobilizing lipase in a wide range of applications.

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Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2

Cited by 67 publications

References 22 publications

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

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

Preparation of Carriers Based on ZnO Nanoparticles Decorated on Graphene Oxide (GO) Nanosheets for Efficient Immobilization of Lipase from Candida rugosa

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