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Registro Completo |
Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
Data corrente: |
20/01/2015 |
Data da última atualização: |
27/11/2023 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
BEZERRA, C. A.; MACEDO, L. L. P.; AMORIM, T. M. L.; SANTOS, V. O.; FRAGOSO, R. da R.; LUCENA, W. A.; MENEGUIM, A. M.; VALENCIA-JIMENEZ, A.; ENGLER, G.; SILVA, M. C. M.; ALBUQUERQUE, E. V. S.; GROSSI-DE-SA, M. F. |
Afiliação: |
FURGS; FURGS; RODRIGO DA ROCHA FRAGOSO, CPAC; WAGNER ALEXANDRE LUCENA, CNPA; IAPAR; UNIVERSITY OF CALDAS, COLOMBIA; INSTITUT NATIONAL DE LA RECHERCHE AGRONOMIQUE, FRANCE; MARIA CRISTINA MATTAR DA SILVA, CENARGEN; ERIKA VALERIA SALIBA ALBUQUERQUE FR, CENARGEN; MARIA FATIMA GROSSI DE SA, CENARGEN. |
Título: |
Molecular cloning and characterization of an α-amylase cDNA highly expressed in major feeding stages of the coffee berry borer, Hypothenemus hampei. |
Ano de publicação: |
2014 |
Fonte/Imprenta: |
Gene, v. 553, n. 1, p. 7-16, Dec. 2014. |
DOI: |
10.1016/j.gene.2014.09.050 |
Idioma: |
Inglês |
Conteúdo: |
Abstract: a-Amylases are common enzymes responsible for hydrolyzing starch. Insect-pests, whose larvae develop in seeds, rely obligatorily on a-amylase activity to digest starch, as their major food source. Considering the relevance of insect a-amylases and the natural a-amylase inhibitors present in seeds to protect from insect damage, we report here the molecular cloning and nucleotide sequence of the full-length AmyHha cDNA of the coffee berry borer, Hypothenemus hampei, a major insect-pest of coffee crops. The AmyHha sequence has 1879 bp, containing a 1458 bp open reading frame, which encodes a predicted protein with 485 amino acid residues, with a predicted molecular mass of 51.2 kDa. The deduced protein showed 55?79% identity to other insect a-amylases, including Anthonomus grandis, Ips typographus and Sitophilus oryzae a-amylases. In depth analysis revealed that the highly conserved three amino acid residues (Asp184, Glu220, and Asp285), which compose the catalytic site are also presented in AmyHha amylase. The AmyHha gene seems to be a single copy in the haploid genome and AmyHha transcription levels were found higher in L2 larvae and adult insects, both corresponding to major feeding phases. Modeling of the AmyHha predicted protein uncovered striking structural similarities to the Tenebrio molitor a-amylase also displaying the same amino acid residues involved in enzyme catalysis (Asp184, Glu220 and Asp285). Since AmyHha gene was mostly transcribed in the intestinal tract of H. hampei larvae, the cognate a-amylase could be considered a high valuable target to coffee bean insect control by biotechnological strategies. MenosAbstract: a-Amylases are common enzymes responsible for hydrolyzing starch. Insect-pests, whose larvae develop in seeds, rely obligatorily on a-amylase activity to digest starch, as their major food source. Considering the relevance of insect a-amylases and the natural a-amylase inhibitors present in seeds to protect from insect damage, we report here the molecular cloning and nucleotide sequence of the full-length AmyHha cDNA of the coffee berry borer, Hypothenemus hampei, a major insect-pest of coffee crops. The AmyHha sequence has 1879 bp, containing a 1458 bp open reading frame, which encodes a predicted protein with 485 amino acid residues, with a predicted molecular mass of 51.2 kDa. The deduced protein showed 55?79% identity to other insect a-amylases, including Anthonomus grandis, Ips typographus and Sitophilus oryzae a-amylases. In depth analysis revealed that the highly conserved three amino acid residues (Asp184, Glu220, and Asp285), which compose the catalytic site are also presented in AmyHha amylase. The AmyHha gene seems to be a single copy in the haploid genome and AmyHha transcription levels were found higher in L2 larvae and adult insects, both corresponding to major feeding phases. Modeling of the AmyHha predicted protein uncovered striking structural similarities to the Tenebrio molitor a-amylase also displaying the same amino acid residues involved in enzyme catalysis (Asp184, Glu220 and Asp285). Since AmyHha gene was mostly transcribed in the intestinal... Mostrar Tudo |
Palavras-Chave: |
Expressão gênica. |
Thesagro: |
Amido; Curculionideo; Hidrolise; Praga de planta. |
Thesaurus Nal: |
Curculionidae; Enzymatic hydrolysis; Gene expression; Insect pests; Starch. |
Categoria do assunto: |
O Insetos e Entomologia |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/115999/1/34279.pdf
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Marc: |
LEADER 02795naa a2200385 a 4500 001 2006141 005 2023-11-27 008 2014 bl uuuu u00u1 u #d 024 7 $a10.1016/j.gene.2014.09.050$2DOI 100 1 $aBEZERRA, C. A. 245 $aMolecular cloning and characterization of an α-amylase cDNA highly expressed in major feeding stages of the coffee berry borer, Hypothenemus hampei.$h[electronic resource] 260 $c2014 520 $aAbstract: a-Amylases are common enzymes responsible for hydrolyzing starch. Insect-pests, whose larvae develop in seeds, rely obligatorily on a-amylase activity to digest starch, as their major food source. Considering the relevance of insect a-amylases and the natural a-amylase inhibitors present in seeds to protect from insect damage, we report here the molecular cloning and nucleotide sequence of the full-length AmyHha cDNA of the coffee berry borer, Hypothenemus hampei, a major insect-pest of coffee crops. The AmyHha sequence has 1879 bp, containing a 1458 bp open reading frame, which encodes a predicted protein with 485 amino acid residues, with a predicted molecular mass of 51.2 kDa. The deduced protein showed 55?79% identity to other insect a-amylases, including Anthonomus grandis, Ips typographus and Sitophilus oryzae a-amylases. In depth analysis revealed that the highly conserved three amino acid residues (Asp184, Glu220, and Asp285), which compose the catalytic site are also presented in AmyHha amylase. The AmyHha gene seems to be a single copy in the haploid genome and AmyHha transcription levels were found higher in L2 larvae and adult insects, both corresponding to major feeding phases. Modeling of the AmyHha predicted protein uncovered striking structural similarities to the Tenebrio molitor a-amylase also displaying the same amino acid residues involved in enzyme catalysis (Asp184, Glu220 and Asp285). Since AmyHha gene was mostly transcribed in the intestinal tract of H. hampei larvae, the cognate a-amylase could be considered a high valuable target to coffee bean insect control by biotechnological strategies. 650 $aCurculionidae 650 $aEnzymatic hydrolysis 650 $aGene expression 650 $aInsect pests 650 $aStarch 650 $aAmido 650 $aCurculionideo 650 $aHidrolise 650 $aPraga de planta 653 $aExpressão gênica 700 1 $aMACEDO, L. L. P. 700 1 $aAMORIM, T. M. L. 700 1 $aSANTOS, V. O. 700 1 $aFRAGOSO, R. da R. 700 1 $aLUCENA, W. A. 700 1 $aMENEGUIM, A. M. 700 1 $aVALENCIA-JIMENEZ, A. 700 1 $aENGLER, G. 700 1 $aSILVA, M. C. M. 700 1 $aALBUQUERQUE, E. V. S. 700 1 $aGROSSI-DE-SA, M. F. 773 $tGene$gv. 553, n. 1, p. 7-16, Dec. 2014.
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Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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Registro Completo
Biblioteca(s): |
Embrapa Agroindústria de Alimentos. |
Data corrente: |
15/03/2012 |
Data da última atualização: |
15/03/2012 |
Tipo da produção científica: |
Resumo em Anais de Congresso |
Autoria: |
DANTER, A. C. R.; MENESES, S. P.; REZENDE, R. S.; TORREZAN, R.; WANG, S. H. |
Afiliação: |
ANDRESSA CHRISTINA RODRIGUES DANTER, UFRRJ; SAMANTHA PILER DE MENESES, UFRRJ; R. S. REZENDE, UFRRJ; RENATA TORREZAN, CTAA; SIN HUEI WANG, UFRRJ. |
Título: |
Uso de soja decorticada tratada termicamente para elaboração do croquete de soja. |
Ano de publicação: |
2011 |
Fonte/Imprenta: |
In: SIMPÓSIO LATINO AMERICANO DE CIÊNCIA DE ALIMENTOS, 9., 2011, Campinas. Ciência de alimentos e qualidade de vida: saúde, meio ambiente e sustentabilidade: resumos. Campinas: UNICAMP, FEA, 2011. 1 CD-ROM. |
Idioma: |
Português |
Palavras-Chave: |
Croquete de soja; Tratamento térmico de soja. |
Thesagro: |
Soja. |
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
Marc: |
LEADER 00720naa a2200193 a 4500 001 1918966 005 2012-03-15 008 2011 bl --- 0-- u #d 100 1 $aDANTER, A. C. R. 245 $aUso de soja decorticada tratada termicamente para elaboração do croquete de soja. 260 $c2011 650 $aSoja 653 $aCroquete de soja 653 $aTratamento térmico de soja 700 1 $aMENESES, S. P. 700 1 $aREZENDE, R. S. 700 1 $aTORREZAN, R. 700 1 $aWANG, S. H. 773 $tIn: SIMPÓSIO LATINO AMERICANO DE CIÊNCIA DE ALIMENTOS, 9., 2011, Campinas. Ciência de alimentos e qualidade de vida: saúde, meio ambiente e sustentabilidade: resumos. Campinas: UNICAMP, FEA, 2011. 1 CD-ROM.
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Embrapa Agroindústria de Alimentos (CTAA) |
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