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| Acesso ao texto completo restrito à biblioteca da Embrapa Soja. Para informações adicionais entre em contato com valeria.cardoso@embrapa.br. |
Registro Completo |
Biblioteca(s): |
Embrapa Soja. |
Data corrente: |
22/07/2019 |
Data da última atualização: |
25/01/2021 |
Tipo da produção científica: |
Capítulo em Livro Técnico-Científico |
Autoria: |
OLIVEIRA, A. B. de; MERTZ-HENNING, L. M.; NEUMAIER, N.; FARIAS, J. R. B.; NEPOMUCENO, A. L. |
Afiliação: |
ARNOLD BARBOSA DE OLIVEIRA, CNPSO; LILIANE MARCIA MERTZ HENNING, CNPSO; NORMAN NEUMAIER, CNPSO; JOSE RENATO BOUCAS FARIAS, CNPSO; ALEXANDRE LIMA NEPOMUCENO, CNPSO. |
Título: |
Estruturas da planta e fases de desenvolvimento. |
Ano de publicação: |
2019 |
Fonte/Imprenta: |
In: OLIVEIRA, A. B. de; LEITE, R. M. V. B. de C.; SEIXAS, C. D. S.; KERN, H. S. Soja: o produtor pergunta, a Embrapa responde. Brasília, DF: Embrapa, 2019. (Coleção 500 perguntas, 500 respostas). |
Páginas: |
p. 25-38. |
Idioma: |
Português |
Thesagro: |
Soja. |
Thesaurus Nal: |
Soybeans. |
Categoria do assunto: |
F Plantas e Produtos de Origem Vegetal |
Marc: |
LEADER 00686naa a2200193 a 4500 001 2110783 005 2021-01-25 008 2019 bl uuuu u00u1 u #d 100 1 $aOLIVEIRA, A. B. de 245 $aEstruturas da planta e fases de desenvolvimento.$h[electronic resource] 260 $c2019 300 $ap. 25-38. 650 $aSoybeans 650 $aSoja 700 1 $aMERTZ-HENNING, L. M. 700 1 $aNEUMAIER, N. 700 1 $aFARIAS, J. R. B. 700 1 $aNEPOMUCENO, A. L. 773 $tIn: OLIVEIRA, A. B. de; LEITE, R. M. V. B. de C.; SEIXAS, C. D. S.; KERN, H. S. Soja: o produtor pergunta, a Embrapa responde. Brasília, DF: Embrapa, 2019. (Coleção 500 perguntas, 500 respostas).
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Embrapa Soja (CNPSO) |
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| Acesso ao texto completo restrito à biblioteca da Embrapa Agroindústria de Alimentos. Para informações adicionais entre em contato com ctaa.biblioteca@embrapa.br. |
Registro Completo
Biblioteca(s): |
Embrapa Agroindústria de Alimentos; Embrapa Agroindústria Tropical. |
Data corrente: |
01/10/2020 |
Data da última atualização: |
02/10/2020 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
A - 1 |
Autoria: |
SANTOS, K. P. dos; SILVA, C. M.; BRIGIDA, A. I. S.; GONÇALVES, L. R. B. |
Afiliação: |
Kimberle Paiva dos Santos, Universidade Federal do Ceará; CAROLINE MELLINGER SILVA, CTAA; ANA IRAIDY SANTA BRIGIDA, CNPAT; Luciana Rocha Barros Gonçalves, Universidade Federal do Ceará. |
Título: |
Modifying alcalase activity and stability by immobilization onto chitosan aiming at the production of bioactive peptides by hydrolysis of tilapia skin gelatin. |
Ano de publicação: |
2020 |
Fonte/Imprenta: |
Process biochemistry, v. 97, p. 27-36, 2020. |
DOI: |
https://doi.org/10.1016/j.procbio.2020.06.019 |
Idioma: |
Inglês |
Conteúdo: |
The protease from Bacillus licheniformis, commercially known as Alcalase (R), was insolubilized and stabilized by immobilization onto activated chitosan. Activation with different agents, such as glutaraldehyde (GLU-Chi), glyoxyl (GLY-Chi) and divinyl sulfone (DVS-Chi) was investigated. The effect of the immobilization protocol, for instance different pH and times, were also evaluated. GLU-Chi showed the highest activity (35.6UNPA/g) with the smallest substrate (N-Boc-L-alanine p-nitrophenyl-ester, NPA), while GLY-Chi showed the highest activity (1.5 UAzocasein/g) using the greatest substrate (azocasein). A 24-h immobilization period was enough to stabilize the enzyme using the three supports under almost all conditions. Operational stability in azocasein hydrolysis was assayed and GLU-Chi showed no activity loss during 5 cycles. DVS-Chi retained around 70 % of its initial activity after the fifth cycle, whereas GLY-Chi activity retained only 10 %. Finally, the biocatalysts were used in the hydrolysis of tilapia skin gelatin aiming the production of peptides with antioxidant activity. The protein hy-drolysates obtained using GLU-Chi presented the highest antioxidant activity (36.7 mu M Trolox Eq). However, the best results of operational stability were obtained using DVS-Chi, which did not lose its initial activity after 3 consecutive cycles of gelatin hydrolysis. |
Palavras-Chave: |
Alcalase; Immobilization; Skin gelatin; Stability. |
Thesagro: |
Tilápia. |
Thesaurus NAL: |
Chitosan; Food technology; Protein hydrolysates. |
Categoria do assunto: |
-- |
Marc: |
LEADER 02237naa a2200265 a 4500 001 2125212 005 2020-10-02 008 2020 bl uuuu u00u1 u #d 024 7 $ahttps://doi.org/10.1016/j.procbio.2020.06.019$2DOI 100 1 $aSANTOS, K. P. dos 245 $aModifying alcalase activity and stability by immobilization onto chitosan aiming at the production of bioactive peptides by hydrolysis of tilapia skin gelatin.$h[electronic resource] 260 $c2020 520 $aThe protease from Bacillus licheniformis, commercially known as Alcalase (R), was insolubilized and stabilized by immobilization onto activated chitosan. Activation with different agents, such as glutaraldehyde (GLU-Chi), glyoxyl (GLY-Chi) and divinyl sulfone (DVS-Chi) was investigated. The effect of the immobilization protocol, for instance different pH and times, were also evaluated. GLU-Chi showed the highest activity (35.6UNPA/g) with the smallest substrate (N-Boc-L-alanine p-nitrophenyl-ester, NPA), while GLY-Chi showed the highest activity (1.5 UAzocasein/g) using the greatest substrate (azocasein). A 24-h immobilization period was enough to stabilize the enzyme using the three supports under almost all conditions. Operational stability in azocasein hydrolysis was assayed and GLU-Chi showed no activity loss during 5 cycles. DVS-Chi retained around 70 % of its initial activity after the fifth cycle, whereas GLY-Chi activity retained only 10 %. Finally, the biocatalysts were used in the hydrolysis of tilapia skin gelatin aiming the production of peptides with antioxidant activity. The protein hy-drolysates obtained using GLU-Chi presented the highest antioxidant activity (36.7 mu M Trolox Eq). However, the best results of operational stability were obtained using DVS-Chi, which did not lose its initial activity after 3 consecutive cycles of gelatin hydrolysis. 650 $aChitosan 650 $aFood technology 650 $aProtein hydrolysates 650 $aTilápia 653 $aAlcalase 653 $aImmobilization 653 $aSkin gelatin 653 $aStability 700 1 $aSILVA, C. M. 700 1 $aBRIGIDA, A. I. S. 700 1 $aGONÇALVES, L. R. B. 773 $tProcess biochemistry$gv. 97, p. 27-36, 2020.
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