Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents

Quilles, José Carlos; Brito, Rafaela Rodrigues de; Borges, J. C.; Aragon, Caio Casale; Fernández‐Lorente, Gloria; Bocchini, Daniela Alonso; Gomes, Eleni; Silva, Roberto da; Boscolo, Maurício; Guisán, José M.

doi:10.1016/j.bej.2014.10.009

Cited by 43 publications

(30 citation statements)

References 20 publications

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“…1a, in the absence of surfactants in an aqueous solution, most lipases are “inactive” because their active centers are covered by a polypeptide chain called lid. However, with the involvement of surfactants, lipases show opened and active form26. Second, aqueous CuSO 4 solution was added to phosphate buffer (0.1 M, pH 7.5) solution containing activated lipases.…”

Section: Resultsmentioning

confidence: 99%

“…Hence, to fully exploit the advantages of immobilized lipases, it is essential to anchor lipases in an active form while they are immobilized. In general, in presence of interface polar–non-polar, the lid of lipase is dislocated and the enzyme shows its opened and active form, which called interfacial activation behavior2627 Moreover, the interfacial activation can induce a dramatic increase in catalytic activity of lipases2829. This effect gave us the vital spark to anchor lipase with active form in hybird nanoflowers by intergrating interfacial activation and self-assembly.…”

mentioning

confidence: 99%

“…Compared to free lipase and hNF-lipase, the activated hNF-lipase exhibited excellent catalytic activity and stability. The superiority of the activated hNF-lipase could be due to the following: (1) Surfactants induce the open conformation of lipase, which makes the active site accessible and, following immobilization, could fix the activated hNF-lipase in the “open conformation”26. (2) Proper interfacial activation could enhance protein rigidity and provide a more effective conformational stabilization of lipase in the activated hNF-lipase28.…”

mentioning

confidence: 99%

“…(3) Nanoflower-like structure of lipase with large surface area and extensive confinement could decrease mass-transfer limitations, which result in higher accessibility of the substrate to the active sites of the enzyme1314. (4) Surfactants could prevent the formation of large lipases aggregates in nanoflowers26, which is helpful to generate uniform architectures with good monodispersity.…”

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confidence: 99%

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Surfactant-activated lipase hybrid nanoflowers with enhanced enzymatic performance

Cui

Zhao

Liu

et al. 2016

Sci Rep

117

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Increasing numbers of materials have been extensively used as platforms for enzyme immobilization to improve catalytic performance. However, activity of the most of the enzymes was declined after immobilization. Here, we develop a surfactant-activated lipase-inorganic flowerlike hybrid nanomaterials with rational design based on interfacial activation and self-assembly. The resulting surfactant-activated lipase-inorganic hybird nanoflower (activated hNF-lipase) exhibited 460% and 200% higher activity than native lipase and conventional lipase-inorganic hybird nanoflower (hNF-lipase). Furthermore, the activated hNF-lipase displayed good reusability due to its monodispersity and mechanical properties, and had excellent long-time stability. The superior catalytic performances were attributed to both the conformational modulation of surfactants and hierarchical structure of nanoflowers, which not only anchored lipases in an active form, but also decreased the enzyme-support negative interaction and mass-transfer limitations. This new biocatalytic system is promising to find widespread use in applications related to biomedicine, biosensor, and biodiesel.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Surfactant-activated lipase hybrid nanoflowers with enhanced enzymatic performance

Cui

Zhao

Liu

et al. 2016

Sci Rep

117

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“…The lipases (triacylglycerol acyl hydrolases, E.C.3.1.1.3) comprise a group of hydrolytic enzymes that act on the organicaqueous interface, catalyzing the hydrolysis of estercarboxylic bonds, present in glycerides. These enzymes cleave specific triglycerides, but may not be completely specific and catalyze the hydrolysis reactions of triacylglycerides that contain different fatty acids in their composition, which may be of great interest for the treatment of effluents with high fat content (Akesson et al, 1983;Quilles et al, 2015;Pecha et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Selection of filamentous fungi producing lipases from residual waters of slaughterhouses

Onofre¹,

Abatti²,

Refosco³

et al. 2017

Afr. J. Biotechnol.

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The exploration and use of lipases produced by microorganisms are in line with societal concerns since they provide clean development options within the standards of environmental sustainability. The objective of this work was therefore to isolate microorganisms with the potential of producing lipases, which could be used in the waste water treatment systems of slaughterhouse units. Waste water samples were collected from the treatment lagoons of a poultry slaughterhouse. The PCA culture medium was used for the isolation of fungi. The pH was adjusted to 6.5 and autoclaved at 1 atm of pressure, for a time of 30 min. The isolated and purified colonies were evaluated in order to obtain lipase producing strains. The results obtained in this study enabled the conclusion that the waste water produced in slaughterhouse has a high microbial load, highlighting bacteria with 6.8 × 10 . Out of this microbial population, six species of lipase producing fungi were isolated, with the fungi Aspergillus flavus and Aspergillus terreus being those that obtained the highest enzymatic indices.

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Pilot‐scale development of core–shell polymer supports for the immobilization of recombinant lipase B from Candida antarctica and their application in the production of ethyl esters from residual fatty acids

Cipolatti

Pinto

Robert

et al. 2018

J of Applied Polymer Sci

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A recombinant lipase B from Candida antarctica (LipB) in Pichia pastoris was synthesized through submerged fermentation using crude glycerin as substrate. The immobilization of this enzyme on the core–shell polymeric supports is an effective alternative for its application. The supports with distinct levels of hydrophobicity were produced through combined suspension and emulsion polymerization in pilot scale. Particles with distinct compositions were synthesized (PMMA/PMMA; PMMA‐co‐DVB/PMMA‐co‐DVB; and PS‐co‐DVB/PS‐co‐DVB) and employed on the immobilization of the produced lipase (LipB) and the commercial enzyme (CalB). The morphological properties (specific area, average pore diameter, specific volume of pores, and hydrophobicity level) and the influence of the polymerization conditions on the morphology of the supports were studied. The thermal stability of such biocatalysts was also investigated in the presence of calcium cation (Ca+2), maintained 100% of the activity after 3 h at 50°C when the PMMA‐co‐DVB/PMMA‐co‐DVB was employed. The synthesized enzyme and supports manufactured in pilot scale were employed successfully for production of esters using residual fatty acids as substrates, adding value to these raw materials and increasing the ranges of possible applications.

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Modulation of the activity and selectivity of the immobilized lipases by surfactants and solvents

Cited by 43 publications

References 20 publications

Surfactant-activated lipase hybrid nanoflowers with enhanced enzymatic performance

Surfactant-activated lipase hybrid nanoflowers with enhanced enzymatic performance

Selection of filamentous fungi producing lipases from residual waters of slaughterhouses

Pilot‐scale development of core–shell polymer supports for the immobilization of recombinant lipase B from Candida antarctica and their application in the production of ethyl esters from residual fatty acids

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