Chitosan activated with divinyl sulfone: a new heterofunctional support for enzyme immobilization. Application in the immobilization of lipase B from Candida antarctica

Pinheiro, Bruna B.; Rios, Nathália Saraiva; Rodríguez‐Aguado, Elena; Fernández-Lafuente, Roberto; Freire, Tiago M.; Fechine, Pierre Basílio Almeida; Santos, José Cleiton Sousa dos; Gonçalves, Luciana Rocha Barros

doi:10.1016/j.ijbiomac.2019.02.145

Cited by 115 publications

(45 citation statements)

References 82 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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“…Furthermore, the enzyme immobilization facilitates catalyst separation at the end of the reaction. The covalent bonding, electrostatic adsorption, encapsulation, and entrapping are common methods for enzyme immobilization [17][18][19].…”

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confidence: 99%

Lipase immobilized on functionalized superparamagnetic few-layer graphene oxide as an efficient nanobiocatalyst for biodiesel production from Chlorella vulgaris bio-oil

Nematian

Shakeri

Salehi

et al. 2020

Biotechnol Biofuels

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Background: Microalgae, due to its well-recognized advantages have gained renewed interest as potentially good feedstock for biodiesel. Production of fatty acid methyl esters (FAMEs) as a type of biodiesel was carried out from Chlorella vulgaris bio-oil. Biodiesel was produced in the presence of nano-biocatalysts composed of immobilized lipase on functionalized superparamagnetic few-layer graphene oxide via a transesterification reaction. A hybrid of few-layer graphene oxide and Fe 3 O 4 (MGO) was prepared and characterized. The MGO was functionalized with 3-aminopropyl triethoxysilane (MGO-AP) as well as with a couple of AP and glutaraldehyde (MGO-AP-GA). The Rhizopus oryzae lipase (ROL) was immobilized on MGO and MGO-AP using electrostatic interactions as well as on MGO-AP-GA using covalent bonding. The supports, MGO, MGO-AP, and MGO-AP-GA, as well as nano-biocatalyst, ROL/MGO, ROL/ MGO-AP, and ROL/MGO-AP-GA, were characterized using FESEM, VSM, FTIR, and XRD. The few-layer graphene oxide was characterized using AFM and the surface charge of supports was evaluated with the zeta potential technique. The nano-biocatalysts assay was performed with an evaluation of kinetic parameters, loading capacity, relative activity, time-course thermal stability, and storage stability. Biodiesel production was carried out in the presence of nanobiocatalysts and their reusability was evaluated in 5 cycles of transesterification reaction. Results: The AFM analysis confirmed the few-layer structure of graphene oxide and VSM also confirmed that all supports were superparamagnetic. The maximum loading of ROL (70.2%) was related to MGO-AP-GA. The highest biodiesel conversion of 71.19% achieved in the presence of ROL/MGO-AP-GA. Furthermore, this nano-biocatalyst could maintain 58.77% of its catalytic performance after 5 cycles of the transesterification reaction and was the best catalyst in the case of reusability. Conclusions: In this study, the synthesized nano-biocatalyst based on bare and functionalized magnetic graphene oxide was applied and optimized in the process of converting microalgae bio-oil to biodiesel for the first time and compared with bare lipase immobilized on magnetic nanoparticles. Results showed that the loading capacity, kinetic parameters, thermal stability, and storage stability improved by the functionalization of MGO. The biocatalysts, which were prepared via covalent bonding immobilization of enzyme generally, showed better characteristics.

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“…Immobilization parameters were evaluated according to the methodology described by Pinheiro et al (2019). Immobilization yield (IY) was defined as the percentage of enzymatic activity that was immobilized, that is, the ratio between the activity of the enzymes retained in the support (initial activity -final activity) and initial activity.…”

Section: Immobilization Parametersmentioning

confidence: 99%

Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method

Moreira

Oliveira

Júnior

et al. 2020

Front. Bioeng. Biotechnol.

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In this communication, it was evaluated the production of fatty acid ethyl ester (FAAE) from the free fatty acids of babassu oil catalyzed by lipase from Rhizomucor miehei (RML) immobilized on magnetic nanoparticles (MNP) coated with 3-aminopropyltriethoxysilane (APTES), Fe 3 O 4 @APTES-RML or RML-MNP for short. MNPs were prepared by co-precipitation coated with 3-aminopropyltriethoxysilane and used as a support to immobilize RML (immobilization yield: 94.7 ± 1.0%; biocatalyst activity: 341.3 ± 1.2 U p−NPB /g), which were also activated with glutaraldehyde and then used to immobilize RML (immobilization yield: 91.9 ± 0.2%; biocatalyst activity: 199.6 ± 3.5 U p−NPB /g). RML-MNP was characterized by X-Ray Powder Diffraction (XRPD), Fourier Transform-Infrared (FTIR) spectroscopy and Scanning Electron Microscope (SEM), proving the incorporation and immobilization of RML on the APTES matrix. In addition, the immobilized biocatalyst presented at 60 • C a half-life 16-19 times greater than that of the soluble lipase in the pH range 5-10. RML and RML-MNP showed higher activity at pH 7; the immobilized enzyme was more active than the free enzyme in the pH range (5-10) analyzed. For the production of fatty acid ethyl ester, under optimal conditions [40 • C, 6 h, 1:1 (FFAs/alcohol)] determined by the Taguchi method, it was possible to obtain conversion of 81.7 ± 0.7% using 5% of RML-MNP.

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Chitosan activated with divinyl sulfone: a new heterofunctional support for enzyme immobilization. Application in the immobilization of lipase B from Candida antarctica

Cited by 115 publications

References 82 publications

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Lipase immobilized on functionalized superparamagnetic few-layer graphene oxide as an efficient nanobiocatalyst for biodiesel production from Chlorella vulgaris bio-oil

Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method

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