Immobilisation studies and catalytic properties of microbial lipase onto styrene–divinylbenzene copolymer

Oliveira, Pedro César Garcia de; Alves, Gizelda M.; Castro, Heizir F. de

doi:10.1016/s1369-703x(99)00061-3

Cited by 106 publications

(44 citation statements)

References 19 publications

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“…The immobilization of enzymes in a solid matrix has been widely investigated and a variety of supporting media has been tested (Lima et al 1996, Oliveira et al 2000. Efforts have been directed towards the finding of good supports for the immobilization of lipases.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the catalytic activity of lipases immobilized on chrysotile for esterification

Silva

Jesus

2003

An. Acad. Bras. Ciênc.

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In the present work, the ester synthesis in organic media catalyzed by lipases immobilized on chrysotile was studied. Lipases of different sources (Mucor javanicus, Pseudomonas cepacia, Rhizopus oryzae, Aspergillus niger and Candida rugosa) were immobilized on chrysotile, an inexpensive magnesium silicate, and used for esterification of hexanoic, octanoic and lauric acid with methanol, ethanol, 1-butanol and 1-octanol at 25 • C in hexane as solvent. The best results were obtained with Mucor javanicus lipase and lauric acid giving yields of 62-97% of ester.

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Section: Introductionmentioning

confidence: 99%

Evaluation of the catalytic activity of lipases immobilized on chrysotile for esterification

Silva

Jesus

2003

An. Acad. Bras. Ciênc.

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“…Using the same enzyme, another report analyzed the effect of the adsorption medium on the biocatalyst performance, using an aqueous solution (with sodium phosphate buffer) and and organic solvent (heptane) [90]. The results were improved when the coupling was performed with heptane.…”

Section: Use Of the Psd-lipase Biocatalysts In Hydrolysis Reactionsmentioning

confidence: 99%

“…Lipase from C. rugosa was immobilized in the presence of heptane on PSD and used to esterify n-butanol and butyric acid [90].…”

Section: Use Of the Psd-lipase Biocatalysts In Esterification Reactionsmentioning

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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“…The enzyme interacts with solid support materials, such as porous glass beads, diatomaceous earth, silica, alumina, ion exchange resins, celites, and biopolymers (de Oliveira et al, 2000;Ghandi et al, 1996;Ivanov and Schneider, 1997;Knezevic et al, 1998), through low energy binding forces such as Van der Waals interactions, hydrophobic interactions, hydrogen bonding, or ionic bonding. The main disadvantage, however, is the relatively low stability of the system due to decreases in activity with time due to enzyme desorption and diffusional limitations (Krajewska, 2004).…”

Section: Immobilization By Adsorptionmentioning

confidence: 99%

A novel reactive perstraction system based on liquid‐core microcapsules applied to lipase‐catalyzed biotransformations

Wyss¹,

Stockar²,

Marison³

2005

Biotech & Bioengineering

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A novel reactive perstraction system has been developed based on liquid-core capsules, involving an enzyme-catalyzed reaction coupled with simultaneous in situ product recovery. Lipase-catalyzed reactions, hydrolysis of triprionin and nitrophenyl laurate, were selected to test the system and demonstrate the feasibility of immobilization of enzymes to the membranes of liquid-core capsules and the ability to extract hydrophobic products of the reaction within the capsule core. The lipase from Candida rugosa was immobilized to the microcapsules by adsorption and by covalent binding through activation with glutaraldehyde. In both cases improved temperature and operational stability were achieved. Both types of immobilization resulted in a basic shift of the pH optimum for activity, from 7.5 to 9.0. The presence of an organic phase within the capsule core allowed direct product separation and lead to a decrease in product inhibition of the lipase-catalyzed reaction.

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Immobilisation studies and catalytic properties of microbial lipase onto styrene–divinylbenzene copolymer

Cited by 106 publications

References 19 publications

Evaluation of the catalytic activity of lipases immobilized on chrysotile for esterification

Evaluation of the catalytic activity of lipases immobilized on chrysotile for esterification

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

A novel reactive perstraction system based on liquid‐core microcapsules applied to lipase‐catalyzed biotransformations

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