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Registro Completo |
Biblioteca(s): |
Embrapa Florestas. |
Data corrente: |
14/05/2021 |
Data da última atualização: |
01/11/2021 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
TOMASI, J. de C.; LIMA, G. G. de; WENDLING, I.; HELM, C. V.; HANSEL, F. A.; GODOY, R. C. B. de; GRUNENNVALDT, R. L.; MELO, T. O. de; TOMAZZOLI, M. M.; DESCHAMPS, C. |
Afiliação: |
JÉSSICA DE CÁSSIA TOMASI, UNIVERSIDADE FEDERAL DO PARANÁ; GABRIEL GOETTEN DE LIMA, UNIVERSIDADE FEDERAL DO PARANÁ; IVAR WENDLING, CNPF; CRISTIANE VIEIRA HELM, CNPF; FABRICIO AUGUSTO HANSEL, CNPF; ROSSANA CATIE BUENO DE GODOY, CNPF; RENATA LÚCIA GRUNENNVALDT, UNIVERSITY OF THE SUNSHINE COAST, AUSTRALIA; TAMIRES OLIVEIRA DE MELO, UNIVERSIDADE FEDERAL DO PARANÁ; MAÍRA MACIEL TOMAZZOLI, UNIVERSIDADE FEDERAL DO PARANÁ; CÍCERO DESCHAMPS, UNIVERSIDADE FEDERAL DO PARANÁ. |
Título: |
Effects of different drying methods on the chemical, nutritional and colour of yerba mate (Ilex paraguariensis) leaves. |
Ano de publicação: |
2021 |
Fonte/Imprenta: |
International Journal of Food Engineering, v. 7, n. 7, p. 551-560, 2021. |
DOI: |
https://doi.org/10.1515/ijfe-2020-0312 |
Idioma: |
Inglês |
Conteúdo: |
This work investigates the effect of different drying processes on chemical, nutritional and leaves colour characteristics for Ilex paraguariensis leaves. These processes were composed of typical drying techniques (roasting + rotary dryer and roasting + conveyor dryer), and cutting-edge techniques (microwave oven [MW], freezedrying (FD) and oven dryer [OD]). The MW can be an alternative technique, this is because the content of phenolic compounds (77 mg/g), antioxidant capacity (DPPH and ABTS) (∼370 and ∼1040 μM TE/g), methylxanthines and caffeoylquinic acids (2?4 mg/g) were similar, and sometimes higher, to the conventional drying processes. Leaves dried with MW also exhibited satisfactory nutritional analysis for protein (16.4%), dietary fibre (52.3%), ash (6.4%), lipid (6.1%) and moisture (5.7%), implying that yerba mate is a potential source of fibre and protein. Furthermore, the MW preserved leaves green colour (high and low scores of b* and a*, respectively). |
Palavras-Chave: |
Erva mate. |
Thesagro: |
Cafeína; Ilex Paraguariensis. |
Thesaurus Nal: |
Bioactive compounds; Caffeine; Yerba mate. |
Categoria do assunto: |
K Ciência Florestal e Produtos de Origem Vegetal |
Marc: |
LEADER 01955naa a2200313 a 4500 001 2131816 005 2021-11-01 008 2021 bl uuuu u00u1 u #d 024 7 $ahttps://doi.org/10.1515/ijfe-2020-0312$2DOI 100 1 $aTOMASI, J. de C. 245 $aEffects of different drying methods on the chemical, nutritional and colour of yerba mate (Ilex paraguariensis) leaves.$h[electronic resource] 260 $c2021 520 $aThis work investigates the effect of different drying processes on chemical, nutritional and leaves colour characteristics for Ilex paraguariensis leaves. These processes were composed of typical drying techniques (roasting + rotary dryer and roasting + conveyor dryer), and cutting-edge techniques (microwave oven [MW], freezedrying (FD) and oven dryer [OD]). The MW can be an alternative technique, this is because the content of phenolic compounds (77 mg/g), antioxidant capacity (DPPH and ABTS) (∼370 and ∼1040 μM TE/g), methylxanthines and caffeoylquinic acids (2?4 mg/g) were similar, and sometimes higher, to the conventional drying processes. Leaves dried with MW also exhibited satisfactory nutritional analysis for protein (16.4%), dietary fibre (52.3%), ash (6.4%), lipid (6.1%) and moisture (5.7%), implying that yerba mate is a potential source of fibre and protein. Furthermore, the MW preserved leaves green colour (high and low scores of b* and a*, respectively). 650 $aBioactive compounds 650 $aCaffeine 650 $aYerba mate 650 $aCafeína 650 $aIlex Paraguariensis 653 $aErva mate 700 1 $aLIMA, G. G. de 700 1 $aWENDLING, I. 700 1 $aHELM, C. V. 700 1 $aHANSEL, F. A. 700 1 $aGODOY, R. C. B. de 700 1 $aGRUNENNVALDT, R. L. 700 1 $aMELO, T. O. de 700 1 $aTOMAZZOLI, M. M. 700 1 $aDESCHAMPS, C. 773 $tInternational Journal of Food Engineering$gv. 7, n. 7, p. 551-560, 2021.
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Registro original: |
Embrapa Florestas (CNPF) |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
Data corrente: |
24/11/2010 |
Data da última atualização: |
04/04/2013 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
A - 2 |
Autoria: |
SOUSA, T. N.; TARAZONA-SANTOS, E. M.; WILSON, D. J.; MADUREIRA, A. P.; FALCAO, P. R. K.; FONTES, C. J. F.; GIL, L. H. S.; FERREIRA, M. U.; CARVALHO, L. H.; BRITO, C. F. A. |
Afiliação: |
TAIS N. SOUSA, CPqRR/FIOCRUZ; EDUARDO M. TARAZONA-SANTOS, ICB/UFMG; DANIEL J. WILSON, University of Chicago; ANA P. MADUREIRA, Universidade Federal de São João del Rei; PAULA REGINA KUSER FALCAO, CNPTIA; COR J. F. FONTES, UFMT; LUIZ H. S. GIL, IPEPATRO; MARCELO U. FERREIRA, USP; LUZIA H. CARVALHO, CPqRR/FIOCRUZ; CRISTIANA F. A. BRITO, CPqRR/FIOCRUZ. |
Título: |
Genetic variability and natural selection at the ligand domain of the Duffy binding protein in Brazilian Plasmodium vivax populations. |
Ano de publicação: |
2010 |
Fonte/Imprenta: |
Malaria Journal, London, v. 9, n. 334, 2010. |
Páginas: |
12 p. |
DOI: |
doi:10.1186/1475-2875-9-334 |
Idioma: |
Inglês |
Conteúdo: |
Background. Plasmodium vivax malaria is a major public health challenge in Latin America, Asia and Oceania, with 130-435 million clinical cases per year worldwide. Invasion of host blood cells by P. vivax mainly depends on a type I membrane protein called Duffy binding protein (PvDBP). The erythrocyte-binding motif of PvDBP is a 170 amino-acid stretch located in its cysteine-rich region II (PvDBPII), which is the most variable segment of the protein. Methods. To test whether diversifying natural selection has shaped the nucleotide diversity of PvDBPII in Brazilian populations, this region was sequenced in 122 isolates from six different geographic areas. A Bayesian method was applied to test for the action of natural selection under a population genetic model that incorporates recombination. The analysis was integrated with a structural model of PvDBPII, and T- and B-cell epitopes were localized on the 3-D structure. Results. The results suggest that: (i) recombination plays an important role in determining the haplotype structure of PvDBPII, and (ii) PvDBPII appears to contain neutrally evolving codons as well as codons evolving under natural selection. Diversifying selection preferentially acts on sites identified as epitopes, particularly on amino acid residues 417, 419, and 424, which show strong linkage disequilibrium. Conclusions. This study shows that some polymorphisms of PvDBPII are present near the erythrocyte-binding domain and might serve to elude antibodies that inhibit cell invasion. Therefore, these polymorphisms should be taken into account when designing vaccines aimed at eliciting antibodies to inhibit erythrocyte invasion. MenosBackground. Plasmodium vivax malaria is a major public health challenge in Latin America, Asia and Oceania, with 130-435 million clinical cases per year worldwide. Invasion of host blood cells by P. vivax mainly depends on a type I membrane protein called Duffy binding protein (PvDBP). The erythrocyte-binding motif of PvDBP is a 170 amino-acid stretch located in its cysteine-rich region II (PvDBPII), which is the most variable segment of the protein. Methods. To test whether diversifying natural selection has shaped the nucleotide diversity of PvDBPII in Brazilian populations, this region was sequenced in 122 isolates from six different geographic areas. A Bayesian method was applied to test for the action of natural selection under a population genetic model that incorporates recombination. The analysis was integrated with a structural model of PvDBPII, and T- and B-cell epitopes were localized on the 3-D structure. Results. The results suggest that: (i) recombination plays an important role in determining the haplotype structure of PvDBPII, and (ii) PvDBPII appears to contain neutrally evolving codons as well as codons evolving under natural selection. Diversifying selection preferentially acts on sites identified as epitopes, particularly on amino acid residues 417, 419, and 424, which show strong linkage disequilibrium. Conclusions. This study shows that some polymorphisms of PvDBPII are present near the erythrocyte-binding domain and might serve to elude antibodies that... Mostrar Tudo |
Palavras-Chave: |
Genetic variability; Modelagem estrutural; Seleção natural; Structural modelling; Variabilidade genética. |
Thesagro: |
Polimorfismo. |
Thesaurus NAL: |
malaria; Natural selection; Plasmodium vivax; Polymorphism. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/80555/1/1475-2875-9-334-4.pdf
|
Marc: |
LEADER 02791naa a2200373 a 4500 001 1867894 005 2013-04-04 008 2010 bl uuuu u00u1 u #d 024 7 $adoi:10.1186/1475-2875-9-334$2DOI 100 1 $aSOUSA, T. N. 245 $aGenetic variability and natural selection at the ligand domain of the Duffy binding protein in Brazilian Plasmodium vivax populations.$h[electronic resource] 260 $c2010 300 $a12 p. 520 $aBackground. Plasmodium vivax malaria is a major public health challenge in Latin America, Asia and Oceania, with 130-435 million clinical cases per year worldwide. Invasion of host blood cells by P. vivax mainly depends on a type I membrane protein called Duffy binding protein (PvDBP). The erythrocyte-binding motif of PvDBP is a 170 amino-acid stretch located in its cysteine-rich region II (PvDBPII), which is the most variable segment of the protein. Methods. To test whether diversifying natural selection has shaped the nucleotide diversity of PvDBPII in Brazilian populations, this region was sequenced in 122 isolates from six different geographic areas. A Bayesian method was applied to test for the action of natural selection under a population genetic model that incorporates recombination. The analysis was integrated with a structural model of PvDBPII, and T- and B-cell epitopes were localized on the 3-D structure. Results. The results suggest that: (i) recombination plays an important role in determining the haplotype structure of PvDBPII, and (ii) PvDBPII appears to contain neutrally evolving codons as well as codons evolving under natural selection. Diversifying selection preferentially acts on sites identified as epitopes, particularly on amino acid residues 417, 419, and 424, which show strong linkage disequilibrium. Conclusions. This study shows that some polymorphisms of PvDBPII are present near the erythrocyte-binding domain and might serve to elude antibodies that inhibit cell invasion. Therefore, these polymorphisms should be taken into account when designing vaccines aimed at eliciting antibodies to inhibit erythrocyte invasion. 650 $amalaria 650 $aNatural selection 650 $aPlasmodium vivax 650 $aPolymorphism 650 $aPolimorfismo 653 $aGenetic variability 653 $aModelagem estrutural 653 $aSeleção natural 653 $aStructural modelling 653 $aVariabilidade genética 700 1 $aTARAZONA-SANTOS, E. M. 700 1 $aWILSON, D. J. 700 1 $aMADUREIRA, A. P. 700 1 $aFALCAO, P. R. K. 700 1 $aFONTES, C. J. F. 700 1 $aGIL, L. H. S. 700 1 $aFERREIRA, M. U. 700 1 $aCARVALHO, L. H. 700 1 $aBRITO, C. F. A. 773 $tMalaria Journal, London$gv. 9, n. 334, 2010.
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