Nanomaterials for biocatalyst immobilization – state of the art and future trends

Cipolatti, Eliane Pereira; Valério, Alexsandra; Henriques, Rosana Oliveira; Moritz, Denise Esteves; Ninow, Jorge Luiz; Freire, Denise Maria Guimarães; Manoel, Evelin Andrade; Fernández-Lafuente, Roberto; Oliveira, Débora de

doi:10.1039/c6ra22047a

Cited by 286 publications

(188 citation statements)

References 170 publications

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“…When the immobilized enzyme was reused, a slight loss of the catalytic activity could be observed, which may be due to the leakage of protein from SBA-15. Considering the operational simplicity of the immobilized enzyme on magnetic nanoparticles [46][47][48], research on using immobilized MML attached onto the magnetic Fe3O4 nanoparticles by covalent attachment for recycling is currently undergoing and will be reported in the future. To test the robustness of the reaction, various substituted salicylaldehydes or indoles have been used for the synthesis of indolyl 4H-chromenes.…”

Section: Resultsmentioning

confidence: 99%

Lipase-Catalyzed Synthesis of Indolyl 4H-Chromenes via a Multicomponent Reaction in Ionic Liquid

et al. 2017

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Section: Resultsmentioning

confidence: 99%

Lipase-Catalyzed Synthesis of Indolyl 4H-Chromenes via a Multicomponent Reaction in Ionic Liquid

et al. 2017

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“…To improve the products separation, successive reuse cycles, and keep the biocatalyst activity and stability during reactions process, different techniques can be used in the immobilization process, such as adsorption [11,12], covalent bonding [13,14], and entrapment [9,[15][16][17]. In the literature, organic and inorganic supports for enzyme immobilization are reported [7,9,10,18], and many studies confirm the potential use of polymers as a support for enzyme immobilization [5,7,15,16,19]. Among the polymers, polystyrene (PS) is a thermoplastic polymer, low cost, that can be easily synthesized and used as support [15].…”

Section: Introductionmentioning

confidence: 99%

Potential application of Thermomyces lanuginosus lipase (TLL) immobilized on nonporous polystyrene particles

Dantas

Valério

Ninow

et al. 2018

Env Prog and Sustain Energy

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The crescent demand for biocatalyst application, associated with the production costs and the need to reduce the dependence for the fossil fuels combined with waste recovery, which could be used as an alternative to resources, increased the interests for the enzyme immobilization. In this work, low‐cost nonporous polystyrene (PS) particles were studied as a support to Thermomyces Lanuginosus lipase (NS‐40116) immobilization. The results showed that immobilized lipase on PS matrix showed better thermal and pH stability when compared to soluble NS‐40116 lipase, with an increase of 84% in the hydrolytic activity at pH 12. Kinetic constants showed that immobilization process increased enzyme specificity by the substrate. In addition, immobilized lipase on PS matrix was effectively applied in the production of free fatty acids from commercial soybean oil demonstrating operational stability after five reuse cycles as well as potential application in the transesterification and esterification reactions by using abdominal chicken fat as substrate. © 2018 American Institute of Chemical Engineers Environ Prog, 38: 608–613, 2019

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“…The immobilization of enzymes on nanoparticles represents another promising strategy for enzyme conjugates. Apart from the benefits in enhanced enzyme activity and stability, new vistas in biocatalysis are opened up …”

Section: Introductionmentioning

confidence: 99%

Enzyme–Polymer Conjugates to Enhance Enzyme Shelf Life in a Liquid Detergent Formulation

Kübelbeck

Mikhael

Keller

et al. 2018

Macromolecular Bioscience

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Herein, the synthesis of enzyme-polymer conjugates is reported. Four different activated polymers (mPEG-aldehyde, mPEG-NHS, maltodextrin-aldehyde, carboxymethyl cellulose aldehyde) are conjugated to the surface of protease, α-amylase, and lipase using two different strategies (reductive amination and alkylation with NHS-activated acid). Although the chemical modification of the enzymes is accompanied by losses in enzyme activity (maximum loss 40%), the covalent attachment of polymers increases the thermal stability and the stability in a standard detergent formulation compared to the unmodified enzymes. The enzyme-polymer conjugates are characterized by asymmetrical-flow field-flow fractionation and differential scanning microcalorimetry. Furthermore, it is demonstrated that conjugated enzymes still show performance in a real washing process. Enzyme-polymer conjugates show a potential as a stabilizing system for enzymes in detergents.

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Nanomaterials for biocatalyst immobilization – state of the art and future trends

Abstract: Advantages, drawbacks and trends in nanomaterials for enzyme immobilization.

Cited by 286 publications

References 170 publications

Lipase-Catalyzed Synthesis of Indolyl 4H-Chromenes via a Multicomponent Reaction in Ionic Liquid

Lipase-Catalyzed Synthesis of Indolyl 4H-Chromenes via a Multicomponent Reaction in Ionic Liquid

Potential application of Thermomyces lanuginosus lipase (TLL) immobilized on nonporous polystyrene particles

Enzyme–Polymer Conjugates to Enhance Enzyme Shelf Life in a Liquid Detergent Formulation

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