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  1. Article: Evaluation of Fischer-Tropsch synthesis to light olefins over Co- and Fe-based catalysts using artificial neural network

    Garona, Higor A. / Cavalcanti, Fabio M. / de Abreu, Thiago F. / Schmal, Martin / Alves, Rita M.B.

    Journal of cleaner production. 2021 Oct. 25, v. 321

    2021  

    Abstract: Currently, energy transition due to fossil fuel negative side effects is taking place. This transition impacts the chemical industry based on light olefins reactions. Plastics, detergents, polymers, and others are mostly produced from such hydrocarbons, ... ...

    Abstract Currently, energy transition due to fossil fuel negative side effects is taking place. This transition impacts the chemical industry based on light olefins reactions. Plastics, detergents, polymers, and others are mostly produced from such hydrocarbons, which are mainly originated from oil-based and highly energy-consuming processes. Fischer-Tropsch Synthesis (FTS) is a strategic technology capable to transform a given carbon source, including natural gas and biomass, into high added-value hydrocarbons. It is affected by several conditions, such as catalyst design and operating conditions and its feasibility requires a good selection of relevant process variables to optimize light olefins yield. In this work, Machine Learning models were used to predict adequate reaction conditions from the catalytic literature data. Three-layer feedforward neural networks were adjusted using a careful selection of operating conditions and catalyst composition as inputs and carbon monoxide conversion, light olefins selectivity, and carbon dioxide yield as outputs. The results indicate neural network prediction efficacy for FTS most relevant variables, such as temperature and catalyst composition. This work presents the novelty of including more variables in the model compared to recent similar studies, such as catalyst support, active phase, and promoters as inputs; and light olefins selectivity and CO₂ yield as outputs. Overall, Fe-based catalyst (standard Fe (1.6 wt%) K/TiO₂) presented the highest light olefins selectivity and yield at optimal conditions (T = 500 °C and 20 wt% of active phase), despite showing the highest emission of carbon dioxide.
    Keywords Fischer-Tropsch reaction ; biomass ; carbon ; carbon dioxide ; carbon monoxide ; catalysts ; chemical industry ; energy ; natural gas ; neural networks ; prediction ; temperature
    Language English
    Dates of publication 2021-1025
    Publishing place Elsevier Ltd
    Document type Article
    ISSN 0959-6526
    DOI 10.1016/j.jclepro.2021.129003
    Database NAL-Catalogue (AGRICOLA)

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  2. Article ; Online: Multiomics Profiling of Toxins in the Venom of the Amazonian Spider

    Nishiduka, Erika S / Abreu, Thiago F / Abukawa, Fernanda Midori / Oliveira, Ursula C / Tardivo, Caio E O / Nascimento, Soraia M / Meissner, Gabriel O / Chaim, Olga M / Juliano, Maria A / Kitano, Eduardo S / Zelanis, André / Serrano, Solange M T / da Silva, Pedro I / Junqueira-de-Azevedo, Inácio L / Nishiyama-Jr, Milton Y / Tashima, Alexandre K

    Journal of proteome research

    2022  Volume 21, Issue 11, Page(s) 2783–2797

    Abstract: Acanthoscurria ... ...

    Abstract Acanthoscurria juruenicola
    MeSH term(s) Animals ; Male ; Female ; Spiders/genetics ; Spiders/metabolism ; Spider Venoms/genetics ; Spider Venoms/chemistry ; Spider Venoms/metabolism ; Cysteine/metabolism ; Proteomics/methods ; Mass Spectrometry/methods ; Proteome/genetics ; Proteome/metabolism ; Peptides/analysis
    Chemical Substances Spider Venoms ; Cysteine (K848JZ4886) ; Proteome ; Peptides
    Language English
    Publishing date 2022-10-19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.2c00593
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Peptidomics of Acanthoscurria gomesiana spider venom reveals new toxins with potential antimicrobial activity.

    Abreu, Thiago F / Sumitomo, Bianca N / Nishiyama, Milton Y / Oliveira, Ursula C / Souza, Gustavo H M F / Kitano, Eduardo S / Zelanis, André / Serrano, Solange M T / Junqueira-de-Azevedo, Inácio / Silva, Pedro I / Tashima, Alexandre K

    Journal of proteomics

    2017  Volume 151, Page(s) 232–242

    Abstract: Acanthoscurria gomesiana is a Brazilian spider from the Theraphosidae family inhabiting regions of Southeastern Brazil. Potent antimicrobial peptides as gomesin and acanthoscurrin have been discovered from the spider hemolymph in previous works. Spider ... ...

    Abstract Acanthoscurria gomesiana is a Brazilian spider from the Theraphosidae family inhabiting regions of Southeastern Brazil. Potent antimicrobial peptides as gomesin and acanthoscurrin have been discovered from the spider hemolymph in previous works. Spider venoms are also recognized as sources of biologically active peptides, however the venom peptidome of A. gomesiana remained unexplored to date. In this work, a MS-based workflow was applied to the investigation of the spider venom peptidome. Data-independent and data-dependent LC-MS/MS acquisitions of intact peptides and of peptides submitted to multiple enzyme digestions, followed by automated chromatographic alignment, de novo analysis, database and homology searches with manual validations showed that the venom is composed by <165 features, with masses ranging from 0.4-15.8kDa. From digestions, 135 peptides were identified from 17 proteins, including three new mature peptides: U1-TRTX-Agm1a, U1-TRTX-Agm2a and U1-TRTX-Agm3a, containing 3, 4 and 3 disulfide bonds, respectively. The toxins U1-TRTX-Agm1a differed by only one amino acid from U1-TRTX-Ap1a from A. paulensis and U1-TRTX-Agm2a was derived from the genicutoxin-D1 precursor from A. geniculata. These toxins have potential applications as antimicrobial agents, as the peptide fraction of A. gomesiana showed activity against Escherichia coli, Enterobacter cloacae and Candida albicans strains. MS data are available via ProteomeXchange Consortium with identifier PXD003884.
    Biological significance: Biological fluids of the Acanthoscurria gomesiana spider are sources of active molecules, as is the case of antimicrobial peptides and acylpolyamines found in the hemolymphs. The venom is also a potential source of toxins with pharmacological and biotechnological applications. However, to our knowledge no A. gomesiana venom toxin structure has been determined to date. Using a combination of high resolution mass spectrometry, transcriptomics and bioinformatics, we employed a workflow to fully sequence, determine the number of disulfide bonds of mature peptides and we found new potential antimicrobial peptides. This workflow is suitable for complete peptide toxin sequencing when handling limited amount of venom samples and can accelerate the discovery of peptides with potential biotechnological applications.
    Language English
    Publishing date 2017-01-16
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2400835-7
    ISSN 1876-7737 ; 1874-3919
    ISSN (online) 1876-7737
    ISSN 1874-3919
    DOI 10.1016/j.jprot.2016.07.012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Peptidomics of Acanthoscurria gomesiana spider venom reveals new toxins with potential antimicrobial activity

    Abreu, Thiago F / Alexandre K. Tashima / André Zelanis / Bianca N. Sumitomo / Eduardo S. Kitano / Gustavo H.M.F. Souza / Inácio Junqueira‐de‐Azevedo / Milton Y. Nishiyama / Pedro I. Silva / Solange M.T. Serrano / Ursula C. Oliveira

    Journal of proteomics. 2017 Jan. 16, v. 151

    2017  

    Abstract: Acanthoscurria gomesiana is a Brazilian spider from the Theraphosidae family inhabiting regions of Southeastern Brazil. Potent antimicrobial peptides as gomesin and acanthoscurrin have been discovered from the spider hemolymph in previous works. Spider ... ...

    Abstract Acanthoscurria gomesiana is a Brazilian spider from the Theraphosidae family inhabiting regions of Southeastern Brazil. Potent antimicrobial peptides as gomesin and acanthoscurrin have been discovered from the spider hemolymph in previous works. Spider venoms are also recognized as sources of biologically active peptides, however the venom peptidome of A. gomesiana remained unexplored to date. In this work, a MS-based workflow was applied to the investigation of the spider venom peptidome. Data-independent and data-dependent LC-MS/MS acquisitions of intact peptides and of peptides submitted to multiple enzyme digestions, followed by automated chromatographic alignment, de novo analysis, database and homology searches with manual validations showed that the venom is composed by <165 features, with masses ranging from 0.4–15.8kDa. From digestions, 135 peptides were identified from 17 proteins, including three new mature peptides: U1-TRTX-Agm1a, U1-TRTX-Agm2a and U1-TRTX-Agm3a, containing 3, 4 and 3 disulfide bonds, respectively. The toxins U1-TRTX-Agm1a differed by only one amino acid from U1-TRTX-Ap1a from A. paulensis and U1-TRTX-Agm2a was derived from the genicutoxin-D1 precursor from A. geniculata. These toxins have potential applications as antimicrobial agents, as the peptide fraction of A. gomesiana showed activity against Escherichia coli, Enterobacter cloacae and Candida albicans strains. MS data are available via ProteomeXchange Consortium with identifier PXD003884.Biological fluids of the Acanthoscurria gomesiana spider are sources of active molecules, as is the case of antimicrobial peptides and acylpolyamines found in the hemolymphs. The venom is also a potential source of toxins with pharmacological and biotechnological applications. However, to our knowledge no A. gomesiana venom toxin structure has been determined to date. Using a combination of high resolution mass spectrometry, transcriptomics and bioinformatics, we employed a workflow to fully sequence, determine the number of disulfide bonds of mature peptides and we found new potential antimicrobial peptides. This workflow is suitable for complete peptide toxin sequencing when handling limited amount of venom samples and can accelerate the discovery of peptides with potential biotechnological applications.
    Keywords Acanthoscurria ; amino acids ; anti-infective agents ; anti-infective properties ; antimicrobial peptides ; bioinformatics ; Candida albicans ; chromatography ; databases ; disulfide bonds ; Enterobacter cloacae ; Escherichia coli ; hemolymph ; mass spectrometry ; proteins ; toxins ; transcriptomics ; venoms ; Brazil
    Language English
    Dates of publication 2017-0116
    Size p. 232-242.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 2400835-7
    ISSN 1876-7737 ; 1874-3919
    ISSN (online) 1876-7737
    ISSN 1874-3919
    DOI 10.1016/j.jprot.2016.07.012
    Database NAL-Catalogue (AGRICOLA)

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  5. Article: Peptidomics of Acanthoscurria gomesiana spider venom reveals new toxins with potential antimicrobial activity

    Abreu, Thiago F. / Bianca N. SumitomoauthorDepartamento de Bioquímica, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, SP, Brazil / Milton Y. NishiyamaauthorLaboratório Especial de Toxinologia Aplicada, Center of Toxins, Immune-Response and Cell Signaling, Instituto Butantan, São Paulo, SP, Brazil / Ursula C. de OliveiraauthorLaboratório Especial de Toxinologia Aplicada, Center of Toxins, Immune-Response and Cell Signaling, Instituto Butantan, São Paulo, SP, Brazil / Gustavo H.M.F. SouzaauthorMass Spectrometry Applications Research & Development Laboratory, Waters Corporation, Sāo Paulo-, SP, Brazil / Eduardo S. KitanoauthorLaboratório Especial de Toxinologia Aplicada, Center of Toxins, Immune-Response and Cell Signaling, Instituto Butantan, São Paulo, SP, Brazil / André ZelanisauthorDepartamento de Ciência e Tecnologia, Universidade Federal de São Paulo, ICT-UNIFESP, São José dos Campos, SP, Brazil / Solange M.T. SerranoauthorLaboratório Especial de Toxinologia Aplicada, Center of Toxins, Immune-Response and Cell Signaling, Instituto Butantan, São Paulo, SP, Brazil / Inácio Junqueira de AzevedoauthorLaboratório Especial de Toxinologia Aplicada, Center of Toxins, Immune-Response and Cell Signaling, Instituto Butantan, São Paulo, SP, Brazil / Pedro I. da SilvaauthorLaboratório Especial de Toxinologia Aplicada, Center of Toxins, Immune-Response and Cell Signaling, Instituto Butantan, São Paulo, SP, Brazil / Alexandre K. TashimaauthorDepartamento de Bioquímica, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, SP, Brazil
    Language English
    Document type Article
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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