LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 5 of total 5

Search options

  1. Article ; Online: A comprehensive review on enzyme-based biosensors: Advanced analysis and emerging applications in nanomaterial-enzyme linkage.

    Melo, Rafael Leandro Fernandes / Neto, Francisco Simão / Dari, Dayana Nascimento / Fernandes, Bruno Caio Chaves / Freire, Tiago Melo / Fechine, Pierre Basílio Almeida / Soares, João Maria / Dos Santos, José Cleiton Sousa

    International journal of biological macromolecules

    2024  Volume 264, Issue Pt 2, Page(s) 130817

    Abstract: Biosensors with nanomaterials and enzymes detect and quantify specific targets in samples, converting recognition into measurable signals. The study explores the intrinsic synergy between these elements for detecting and quantifying particular targets in ...

    Abstract Biosensors with nanomaterials and enzymes detect and quantify specific targets in samples, converting recognition into measurable signals. The study explores the intrinsic synergy between these elements for detecting and quantifying particular targets in biological and environmental samples, with results demonstrated through bibliometric analysis and a comprehensive review of enzyme-based biosensors. Using WoS, 57,331 articles were analyzed and refined to 880. Key journals, countries, institutions, and relevant authors were identified. The main areas highlighted the multidisciplinary nature of the field, and critical keywords identified five thematic clusters, revealing the primary nanoparticles used (CNTs, graphene, AuNPs), major application fields, basic application themes, and niche topics such as sensitive detection, peroxidase activity, and quantum dot utilization. The biosensor overview covered nanomaterials and their primary applications, addressing recent advances and inherent challenges. Patent analysis emphasized the U.S. leadership in the industrial sector, contrasting with China's academic prominence. Future studies should focus on enhancing biosensor portability and analysis speed, with challenges encompassing efficient integration with recent technologies and improving stability and reproducibility in the nanomaterial-enzyme interaction.
    MeSH term(s) Gold ; Reproducibility of Results ; Metal Nanoparticles ; Nanostructures ; Biosensing Techniques/methods
    Chemical Substances Gold (7440-57-5)
    Language English
    Publishing date 2024-03-11
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2024.130817
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article ; Online: Enhancing biocatalyst performance through immobilization of lipase (Eversa® Transform 2.0) on hybrid amine-epoxy core-shell magnetic nanoparticles.

    Melo, Rafael Leandro Fernandes / Freire, Tiago Melo / Valério, Roberta Bussons Rodrigues / Neto, Francisco Simão / de Castro Bizerra, Viviane / Fernandes, Bruno Caio Chaves / de Sousa Junior, Paulo Gonçalves / da Fonseca, Aluísio Marques / Soares, João Maria / Fechine, Pierre Basílio Almeida / Dos Santos, José Cleiton Sousa

    International journal of biological macromolecules

    2024  Volume 264, Issue Pt 2, Page(s) 130730

    Abstract: Magnetic nanoparticles were functionalized with polyethylenimine (PEI) and activated with epoxy. This support was used to immobilize Lipase (Eversa® Transform 2.0) (EVS), optimization using the Taguchi method. XRF, SEM, TEM, XRD, FTIR, TGA, and VSM ... ...

    Abstract Magnetic nanoparticles were functionalized with polyethylenimine (PEI) and activated with epoxy. This support was used to immobilize Lipase (Eversa® Transform 2.0) (EVS), optimization using the Taguchi method. XRF, SEM, TEM, XRD, FTIR, TGA, and VSM performed the characterizations. The optimal conditions were immobilization yield (I.Y.) of 95.04 ± 0.79 %, time of 15 h, ionic load of 95 mM, protein load of 5 mg/g, and temperature of 25 °C. The maximum loading capacity was 25 mg/g, and its stability in 60 days of storage showed a negligible loss of only 9.53 % of its activity. The biocatalyst demonstrated better stability at varying temperatures than free EVS, maintaining 28 % of its activity at 70 °C. It was feasible to esterify free fatty acids (FFA) from babassu oil with the best reaction of 97.91 % and ten cycles having an efficiency above 50 %. The esterification of produced biolubricant was confirmed by NMR, and it displayed kinematic viscosity and density of 6.052 mm
    MeSH term(s) Lipase/chemistry ; Enzymes, Immobilized/chemistry ; Magnetite Nanoparticles ; Plant Oils/chemistry ; Esterification ; Enzyme Stability
    Chemical Substances Lipase (EC 3.1.1.3) ; Enzymes, Immobilized ; Magnetite Nanoparticles ; Plant Oils
    Language English
    Publishing date 2024-03-10
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2024.130730
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  3. Article ; Online: Research Progress and Trends on Utilization of Lignocellulosic Residues as Supports for Enzyme Immobilization via Advanced Bibliometric Analysis.

    Neto, Francisco Simão / Fernandes de Melo Neta, Maria Marliete / Sales, Misael Bessa / Silva de Oliveira, Francisco Arisson / de Castro Bizerra, Viviane / Sanders Lopes, Ada Amélia / de Sousa Rios, Maria Alexsandra / Santos, José Cleiton Sousa Dos

    Polymers

    2023  Volume 15, Issue 9

    Abstract: Lignocellulosic biomasses are used in several applications, such as energy production, materials, and biofuels. These applications result in increased consumption and waste generation of these materials. However, alternative uses are being developed to ... ...

    Abstract Lignocellulosic biomasses are used in several applications, such as energy production, materials, and biofuels. These applications result in increased consumption and waste generation of these materials. However, alternative uses are being developed to solve the problem of waste generated in the industry. Thus, research is carried out to ensure the use of these biomasses as enzymatic support. These surveys can be accompanied using the advanced bibliometric analysis tool that can help determine the biomasses used and other perspectives on the subject. With this, the present work aims to carry out an advanced bibliometric analysis approaching the main studies related to the use of lignocellulosic biomass as an enzymatic support. This study will be carried out by highlighting the main countries/regions that carry out productions, research areas that involve the theme, and future trends in these areas. It was observed that there is a cooperation between China, USA, and India, where China holds 28.07% of publications in this area, being the country with the greatest impact in the area. Finally, it is possible to define that the use of these new supports is a trend in the field of biotechnology.
    Language English
    Publishing date 2023-04-26
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2527146-5
    ISSN 2073-4360 ; 2073-4360
    ISSN (online) 2073-4360
    ISSN 2073-4360
    DOI 10.3390/polym15092057
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  4. Article ; Online: Recent applications and future prospects of magnetic biocatalysts.

    Melo, Rafael Leandro Fernandes / Sales, Misael Bessa / de Castro Bizerra, Viviane / de Sousa Junior, Paulo Gonçalves / Cavalcante, Antônio Luthierre Gama / Freire, Tiago Melo / Neto, Francisco Simão / Bilal, Muhammad / Jesionowski, Teofil / Soares, João Maria / Fechine, Pierre Basílio Almeida / Dos Santos, José Cleiton Sousa

    International journal of biological macromolecules

    2023  Volume 253, Issue Pt 3, Page(s) 126709

    Abstract: Magnetic biocatalysts combine magnetic properties with the catalytic activity of enzymes, achieving easy recovery and reuse in biotechnological processes. Lipases immobilized by magnetic nanoparticles dominate. This review covers an advanced bibliometric ...

    Abstract Magnetic biocatalysts combine magnetic properties with the catalytic activity of enzymes, achieving easy recovery and reuse in biotechnological processes. Lipases immobilized by magnetic nanoparticles dominate. This review covers an advanced bibliometric analysis and an overview of the area, elucidating research advances. Using WoS, 34,949 publications were analyzed and refined to 450. The prominent journals, countries, institutions, and authors that published the most were identified. The most cited articles showed research hotspots. The analysis of the themes and keywords identified five clusters and showed that the main field of research is associated with obtaining biofuels derived from different types of sustainable vegetable oils. The overview of magnetic biocatalysts showed that these materials are also employed in biosensors, photothermal therapy, environmental remediation, and medical applications. The industry shows a significant interest, with the number of patents increasing. Future studies should focus on immobilizing new lipases in unique materials with magnetic profiles, aiming to improve the efficiency for various biotechnological applications.
    MeSH term(s) Enzymes, Immobilized ; Lipase ; Magnetics ; Nanoparticles ; Magnetic Phenomena
    Chemical Substances Enzymes, Immobilized ; Lipase (EC 3.1.1.3)
    Language English
    Publishing date 2023-09-09
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2023.126709
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  5. Article: Chemical modification of clay nanocomposites for the improvement of the catalytic properties of Lipase A from Candida antarctica

    Cavalcante, Antônio Luthierre Gama / Chaves, Anderson Valério / Fechine, Pierre Basílio Almeida / Holanda Alexandre, Jeferson Yves Nunes / Freire, Tiago Melo / Davi, Dalila Maria Barbosa / Neto, Francisco Simão / de Sousa, Isamayra Germano / da Silva Moreira, Katerine / de Oliveira, André Luiz Barros / de Mattos, Marcos Carlos / Oliveira, Maria Conceição Ferreira / de Brito, Maria Vieira / Ballereau, Stéphanie / Bernardes-Génisson, Vania / da Fonseca, Aluísio Marques / dos Santos, José C.S.

    Process biochemistry. 2022 May 20,

    2022  

    Abstract: Kaolin is a mineral composed of hydrated aluminum silicates, clayey and with high bioavailability. The choice of this mineral as immobilization matrix took into account these aspects mentioned above and its high surface area conducive to enzymatic ... ...

    Abstract Kaolin is a mineral composed of hydrated aluminum silicates, clayey and with high bioavailability. The choice of this mineral as immobilization matrix took into account these aspects mentioned above and its high surface area conducive to enzymatic immobilization, containing many OH⁻ binding groups on its surface. Subsequently, the kaolin was functionalized with carboxymethylcellulose and polyethyleneimine (K-CMC-BPEI) and activated with Glutaraldehyde (K-CMC-BPEI-GLU) as a support to immobilize CAL-A. The K-CMC-BPEI-GLU@CAL-A was characterized by X-Ray Diffraction (XRD), Fourier Transform Infrared Spectroscopy (FTIR), Thermogravimetry (TGA), and Scanning Electron Microscopy (SEM). K-CMC-BPEI-GLU@CAL-A, in the temperature range of 50 - 80 ºC, has a half-life 2 to 3 times longer than soluble CAL-A, that is, the immobilization process conferred greater stability thermal to the biocatalyst. Furthermore, docking studies showed that the immobilization of CAL-A on the support surface was favorable, since CAL-A has binding affinity to the protein-anchored ligand, estimated at -4.3 to -3.7kcal/mol. Experiments were performed to verify the catalytic potential of K-CMC-BPEI-GLU@CAL-A at a kinetic resolution of rac-1-(triisopropylsilyl) penta-1,4-diyn-3-ol (1) in an organic medium via an acylation reaction. All experiments yielded the product ((R)-1-Ac) with an excellent enantiomeric excess (ee >99%) and enantioselectivity (E >200).
    Keywords Fourier transform infrared spectroscopy ; Pseudozyma antarctica ; acylation ; aluminum ; bioavailability ; biocatalysts ; carboxylic ester hydrolases ; carboxymethylcellulose ; clay ; electron microscopy ; enantioselectivity ; glutaraldehyde ; half life ; kaolin ; ligands ; nanocomposites ; polyethyleneimine ; surface area ; temperature ; thermogravimetry
    Language English
    Dates of publication 2022-0520
    Publishing place Elsevier Ltd
    Document type Article
    Note Pre-press version
    ISSN 1359-5113
    DOI 10.1016/j.procbio.2022.05.020
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

To top