Interfacially activated lipases against hydrophobic supports: Effect of the support nature on the biocatalytic properties

Fernández‐Lorente, Gloria; Cabrera, Zaida; Godoy, César A.; Fernández‐Lafuente, Roberto; Palomo, José M.; Guisán, José M.

doi:10.1016/j.procbio.2008.05.009

Cited by 211 publications

(188 citation statements)

References 40 publications

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“…Triton X-100 acts as the opposite, improving desorption because of the competition with lipases for hydrophobic regions of silica gel (Palomo et al 2004). These results suggested that the nature of adsorption of B. bassiana lipase on silica gel was hydrophobic probably by interfacial activation (Fernandez-Lorente et al 2008). Operational stability Adsorbed lipase shows a great reuse capacity in organic solvents because of the less leakage of enzyme from support (Kumari et al 2008;Doukyu and Ogino 2010).…”

Section: Effect Of Ph and Temperature On The Activity Of Fl And Ilsmentioning

confidence: 91%

“…Lipases (glycerol ester hydrolases, E.C.3.1.1.3) are considered the most promising group of biocatalysts due to their ability to act in different types of reactions as hydrolysis, interesterification, esterification, alcoholysis, acidolysis and aminolysis (Hasan et al 2009). They can act on a wide range of substrates and show interesting properties such as regio-and stereo-specificity, and chemoselectivity that allows their several applications, including the production of detergents, wastewater treatment, textile and leather tanning (Castro-Ochoa et al 2005;Fernandez-Lorente et al 2008). Lipases on immobilized forms have been successfully applied in organic catalysis production of flavorings, pharmaceuticals and agrochemicals (Abbas and Comeau 2003).…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of Beauveria bassiana Lipase on Silica Gel by Physical Adsorption

Sugahara

Varéa

2014

Braz. arch. biol. technol.

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Section: Effect Of Ph and Temperature On The Activity Of Fl And Ilsmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Immobilization of Beauveria bassiana Lipase on Silica Gel by Physical Adsorption

Sugahara

Varéa

2014

Braz. arch. biol. technol.

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“…However, this mechanism of action causes lipases to become an exception among water soluble proteins: while the surface of the closed form is fairly hydrophilic, the open form has a huge hydrophobic pocket. This permits that the lipases may suffer interfacial activation with different hydrophobic surfaces: a drop of oil (Verger, 1997) or a hydrophobic support (Bastida et al, 1998, FernandezLafuente et al, 1998, Garcia-Galan et al, 2014 (Fernandez-Lorente et al, 2008, Fernández-Lorente et al, 2007 and to purify it .…”

Section: 1-the Case Of Lipases Immobilization Via Interfacial Activmentioning

confidence: 99%

Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts

Barbosa

Ortíz

Berenguer-Murcia

et al. 2015

Biotechnology Advances

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613

318

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Enzyme immobilization and purification are two steps that are usually required in the development of any industrial biocatalyst. In this review, we detail the efforts performed to couple the purification and the immobilization of industrial enzymes in a single step. The use of antibodies (versus the target enzyme or versus some domains), the development of specific domains with affinity for some specific supports or just to increase the affinity for standard ones (ionic exchangers, silicates) will be revised. We will show how the control of the immobilization conditions may convert some unspecific supports in largely specific ones. The development of tailormade heterofunctional supports as a tool to immobilize-stabilize-purify some proteins will be discussed in deep, using low concentration of adsorbents groups and a dense layer of groups able to give an intense multipoint covalent attachment. The final coupling of mutagenesis and tailor made supports will be a the last part of the review.

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“…Moreover, it has been reported that the hydrophobicity and internal morphology of the support may be used to tune enzyme properties [87].…”

Section: Lipase Immobilization Via Interfacial Acti-vation On Hydrophmentioning

confidence: 99%

Immobilization of Proteins in Poly-Styrene-Divinylbenzene Matrices: Functional Properties and Applications

Rafael¹,

Hernández²,

Barbosa³

et al. 2015

COC

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Supports based on poly-styrene-divinylbenzene (PSD) are commercially available since a long time ago. However, they are not commonly used as enzyme immobilization matrices. The main reason for this lies in the negative effect of the very hydrophobic surface on enzyme stability that produces the instantaneous enzyme inactivation in many instances. However, they have recently regained some impact on enzyme immobilization. They are easy to modify, and have been prepared with different modifiers. We will pay special attention to the coating of these supports with ionic liquids, which permits to have the ionic liquid phase anchored to the solid and modulate the enzyme properties without risk of losing these expensive and potentially toxic compounds. Thus, this review will present the covalent or physical immobilization of enzymes on PSD supports, submitted to different modifications. Moreover, lipases immobilized via interfacial activation on some naked PSD supports have shown some unexpected improvement in their catalytic properties, with uses in reactions like hydrolysis, esterification or transesterification.

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Interfacially activated lipases against hydrophobic supports: Effect of the support nature on the biocatalytic properties

Cited by 211 publications

References 40 publications

Immobilization of Beauveria bassiana Lipase on Silica Gel by Physical Adsorption

Immobilization of Beauveria bassiana Lipase on Silica Gel by Physical Adsorption

Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts

Immobilization of Proteins in Poly-Styrene-Divinylbenzene Matrices: Functional Properties and Applications

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