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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
06/05/2016 |
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Data da última atualização: |
24/03/2022 |
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Autoria: |
COSTA, E. O.; RIBEIRO, A. R.; MELVILLE, P. A.; SANTIS-PRADA, M. |
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Título: |
Avaliação da eficácia da anti-sepsia pós-ordenha no controle de mastite aplicando o modelo "split herd". |
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Ano de publicação: |
1999 |
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Fonte/Imprenta: |
Revista Napgama, v. 2, n. 2, p. 4-9, mar./abr. 1999. |
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Idioma: |
Português |
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Palavras-Chave: |
Assepsia; Controle; Pos-dipping; Pos-dipping teat; Pós-ordenha; Split herd. |
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Thesagro: |
Desinfecção; Desinfetante; Mamite. |
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Thesaurus Nal: |
Antiseptics; Mastitis. |
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Categoria do assunto: |
H Saúde e Patologia |
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Marc: |
LEADER 00764naa a2200277 a 4500
001 2044526
005 2022-03-24
008 1999 bl uuuu u00u1 u #d
100 1 $aCOSTA, E. O.
245 $aAvaliação da eficácia da anti-sepsia pós-ordenha no controle de mastite aplicando o modelo "split herd".
260 $c1999
650 $aAntiseptics
650 $aMastitis
650 $aDesinfecção
650 $aDesinfetante
650 $aMamite
653 $aAssepsia
653 $aControle
653 $aPos-dipping
653 $aPos-dipping teat
653 $aPós-ordenha
653 $aSplit herd
700 1 $aRIBEIRO, A. R.
700 1 $aMELVILLE, P. A.
700 1 $aSANTIS-PRADA, M.
773 $tRevista Napgama$gv. 2, n. 2, p. 4-9, mar./abr. 1999.
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Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
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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
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Biblioteca(s): |
Embrapa Agroindústria de Alimentos; Embrapa Agroindústria Tropical. |
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Data corrente: |
01/10/2020 |
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Data da última atualização: |
02/10/2020 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
SANTOS, K. P. dos; SILVA, C. M.; BRIGIDA, A. I. S.; GONÇALVES, L. R. B. |
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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. |
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Título: |
Modifying alcalase activity and stability by immobilization onto chitosan aiming at the production of bioactive peptides by hydrolysis of tilapia skin gelatin. |
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Ano de publicação: |
2020 |
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Fonte/Imprenta: |
Process biochemistry, v. 97, p. 27-36, 2020. |
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DOI: |
https://doi.org/10.1016/j.procbio.2020.06.019 |
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Idioma: |
Inglês |
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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. |
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Palavras-Chave: |
Alcalase; Immobilization; Skin gelatin; Stability. |
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Thesagro: |
Tilápia. |
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Thesaurus NAL: |
Chitosan; Food technology; Protein hydrolysates. |
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Categoria do assunto: |
-- |
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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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Embrapa Agroindústria de Alimentos (CTAA) |
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