| |
|
|
 | 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 |
|
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.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Agroindústria de Alimentos (CTAA) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
| Acesso ao texto completo restrito à biblioteca da Embrapa Recursos Genéticos e Biotecnologia. Para informações adicionais entre em contato com cenargen.biblioteca@embrapa.br. |
Registro Completo
|
Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
|
Data corrente: |
11/11/1994 |
|
Data da última atualização: |
09/05/1997 |
|
Autoria: |
EIRA, M. T. S.; SALOMAO, A. N.; CUNHA, R. da; MELLO, C. M. C. de; TANAKA, D. M. |
|
Afiliação: |
EMBRAPA-CENARGEN. |
|
Título: |
Conservacao de sementes de Copaifera langsdorffii Desf. Leguminosae. |
|
Ano de publicação: |
1992 |
|
Fonte/Imprenta: |
Revista do Instituto Florestal, Sao Paulo, v.4, p.523-526, 1992. Ed. especial. |
|
Idioma: |
Português |
|
Notas: |
Apresentado no 2º Congresso Nacional Sobre Essências Nativas, São Paulo, SP, 1992. |
|
Palavras-Chave: |
Seed conservation. |
|
Thesagro: |
Conservação; Copaifera Langsdorffii; Semente. |
|
Categoria do assunto: |
-- |
|
Marc: |
LEADER 00708naa a2200217 a 4500
001 1171175
005 1997-05-09
008 1992 bl uuuu u00u1 u #d
100 1 $aEIRA, M. T. S.
245 $aConservacao de sementes de Copaifera langsdorffii Desf. Leguminosae.
260 $c1992
500 $aApresentado no 2º Congresso Nacional Sobre Essências Nativas, São Paulo, SP, 1992.
650 $aConservação
650 $aCopaifera Langsdorffii
650 $aSemente
653 $aSeed conservation
700 1 $aSALOMAO, A. N.
700 1 $aCUNHA, R. da
700 1 $aMELLO, C. M. C. de
700 1 $aTANAKA, D. M.
773 $tRevista do Instituto Florestal, Sao Paulo$gv.4, p.523-526, 1992. Ed. especial.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
Fechar
|
| Expressão de busca inválida. Verifique!!! |
|
|
