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| Registros recuperados : 8 | |
| 5. |  | SANTOS, K. P. dos; LIMA, Y. S.; BONFIM, B. R. de S.; MARINHO, A. M. C.; RIBEIRO, M. de F. Nicho trófico de Abelha-branca (Frieseomelitta doederelini) na região do Submédio do Vale do São Francisco. In: JORNADA DE INICIAÇÃO CIENTÍFICA DA EMBRAPA SEMIÁRIDO, 12., 2017, Petrolina. Anais... Petrolina: Embrapa Semiárido, 2017. p. 219-225. (Embrapa Semiárido. Documentos, 279).| Biblioteca(s): Embrapa Semiárido. |
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| 6. | | MATOS, R. R. S. da S.; LOPES, P. R. C.; CAVALCANTE, L. F.; OLIVEIRA, I. V. de M.; SANTOS, K. P. dos. Atributos químicos de qualidade de frutos de caquizeiro tratados com cianamida hidrogenada em clima Semiárido. In: CONGRESSO BRASILEIRO DE FRUTICULTURA, 26., 2019, Juazeiro, BA/Petrolina, PE. Fruticultura de precisão: desafios e oportunidades - anais. Petrolina: Embrapa Semiárido: UNIVASF: SBF, 2019. p. 1071-1074| Biblioteca(s): Embrapa Semiárido. |
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| 7. | | BRIGIDA, A. I. S.; SANTOS, K. P. dos; FARIA, L. R.; GONÇALVES, L. R. B.; SILVA, C. M.; AZEVEDO, T. de L. Alcalase immobilization for tilapia skin gelatin Hydrolysis. In: SIMPÓSIO NACIONAL DE BIOPROCESSOS, 21.; SIMPÓSIO DE HIDRÓLISE ENZIMÁTICA DE BIOMASSA, 12., 2017, Aracaju, SE. [Proceedings ...]. São Paulo: Associação Brasileira de Engenharia Química, 2017. SINAFERM; SHEB. 3 a 6 de setembro. Seção Trabalhos. Ref. 56412.| Biblioteca(s): Embrapa Agroindústria de Alimentos. |
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| 8. | | RIBEIRO, M. de F.; ALMEIDA, M. de S.; SOUZA, R. L. V. de; MARIANO, A. M. C.; SANTOS, K. P. dos; GALVÃO, M. N.; SILVA, C. W. da. Spathodea campanulata (Bignoniaceae): flower visitors and nectar characteristics. In: ENCONTRO SOBRE AS ABELHAS, 12., 2018, Uberlândia. Anais... Uberlândia: Universidade Federal de Uberlândia, 2018. p. 211.| Biblioteca(s): Embrapa Semiárido. |
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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 02238naa 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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