Biotechnological potential of lipases from Pseudomonas: Sources, properties and applications

Rios, Nathália Saraiva; Pinheiro, Bruna B.; Pinheiro, Maísa Pessoa; Bezerra, Rayanne Mendes; Santos, José Cleiton Sousa dos; Gonçalves, Luciana Rocha Barros

doi:10.1016/j.procbio.2018.09.003

Cited by 122 publications

(64 citation statements)

References 237 publications

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“…18 However, immobilization is one of the important ways for enzymes to become stable. [19][20][21][22][23] Many methods of immobilization are described and used in the literature to circumvent the possible instability problems of the enzymes as well as to optimize the various applications. In recent years, the empirical use of these immobilization techniques (for example, covalent bonding, 24 physical adsorption, 25 ionic adsorption, 26 crosslinking, 27 encapsulation, 28 etc) and their influences on the specificity, activity and stability of the enzymatic molecules, as well as the usability of the biocatalysts for application-related [29][30][31] reactions.…”

Section: Enzyme Immobilizationmentioning

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: Enzyme Immobilizationmentioning

confidence: 99%

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Reis

Sousa

Serpa

et al. 2019

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“…In this first approach, we have tried to build a three-layer biocatalyst using the lipase from Pseudomonas fluorescens (PFL). This enzyme is very popular in literature [27][28][29]. To simplify the In this first approach, we have tried to build a three-layer biocatalyst using the lipase from Pseudomonas fluorescens (PFL).…”

Section: Introductionmentioning

confidence: 99%

Increasing the Enzyme Loading Capacity of Porous Supports by a Layer-by-Layer Immobilization Strategy Using PEI as Glue

et al. 2019

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A new strategy to increase the enzyme-loading capacity of porous supports was investigated. Lipase from Pseudomonas fluorescens (PFL) was immobilized on octyl-agarose (OA) beads and treated with polyethyleneimine (PEI). Then, PFL was immobilized on the previous PFL layer. Next, the biocatalyst was coated with PEI and a third layer of PFL was added. Sodium dodecyl sulfate polyacrylamide electrophoresis showed that the amount of PFL proportionally increased with each enzyme layer; however, the effects on biocatalyst activity were not as clear. Hydrolyzing 50 mM of triacetin at 25 °C, the activity of the three-layer biocatalyst was even lower than that of the bi-layer one; on the contrary its activity was higher when the activity was measured at 4 °C in the presence of 30% acetonitrile (that reduced the activity and thus the relevance of the substrate diffusion limitations). That is, the advantage of the multilayer formation depends on the specific activity of the enzyme and on the diffusion limitations of the substrate. When octyl agarose (OA)-PFL-PEI-PFL preparation was treated with glutaraldehyde, the activity was reduced, although the enzyme stability increased and the immobilization of the last PFL layer offered results similar to the one obtained using the three-layer preparation without glutaraldehyde modification (90%).

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“…In this new research, we analyze the possibility of co-immobilizing the lipases from Pseudomonas fluorescens (PFL), and RML and the phospholipase LU. These enzymes are very interesting ones, utilized in many biocatalytic reactions [50,51,53,54]. All of them have been immobilized on octyl agarose and glyoxyl-octyl agarose with good results [45,55].…”

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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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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Biotechnological potential of lipases from Pseudomonas: Sources, properties and applications

Cited by 122 publications

References 237 publications

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Increasing the Enzyme Loading Capacity of Porous Supports by a Layer-by-Layer Immobilization Strategy Using PEI as Glue

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

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