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Registro Completo |
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Biblioteca(s): |
Embrapa Gado de Corte. |
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Data corrente: |
23/01/2020 |
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Data da última atualização: |
23/01/2020 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
SILVA, P. O. da; GUIMARÃES, N. C. de A.; SERPA, J. D. M.; MASUI, D. C.; MARCHETTI, C. R.; VERBISCK, N. V.; ZANOELO, F. F.; RULLER, R.; GIANNESI, G. C. |
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Afiliação: |
Patricia Oliveira da Silva, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; Nelciele Cavalieri de Alencar Guimarães, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; John Dayvan Maidana Serpa, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; Douglas Chodi Masui, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; Clarice Rossatto Marchetti, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; NEWTON VALERIO VERBISCK, CNPGC; Fabiana Fonseca Zanoelo, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; Roberto Ruller, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos; Giovana Cristina Giannesi, Universidade Federal de Mato Grosso do Sul - UFMS/Laboratório de Bioquímica e Microorganismos. |
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Título: |
Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis. |
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Ano de publicação: |
2019 |
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Fonte/Imprenta: |
Biocatalysis and Agricultural Biotechnology, v. 21, 2019. |
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Idioma: |
Inglês |
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Conteúdo: |
The endo-xylanase from Aspergillus japonicus (UFMS 48.136) was purified in a single step using carboximethylcellulose chromatographic column and applied in fruit juice clarification process and fruit peel waste hydrolysis. This purification procedure resulted in 38.9-fold purification of endo-xylanase with 83.3% final yield. MALDITOF analysis confirmed the molecular mass of 32 kDa. The optimal purified endo-xylanase activity was at a range of pH from 5.0 to 6.0 and from 50 to 60 +-C, retaining more than 70% of its activity at all pH studied (3.0?8.0) for 24 h at room temperature. The A. japonicus endo-xylanolytic activity stimulation curve was assayed in the presence of different birchwood xylan concentrations (ranging from 0.02 to 0.5% w/v) and the endoxylanase activity presented a Vmax of 467.4 +- 30.38 μmol/min/mg, with a km of 2.59 +- 0.17 mg/mL, a kcat of 253.95 +- 16.51 s -1 and a kcat/km value of 98.05 +- 4.41 mL s -1 mg -1. The endo-xylanase was activated by Mn2þ (34.5%) and inhibited by Cu2þ (56.9%). The endo-xylanase was activated by β-mercaptoethanol, Triton X-100, Tween-20, Tween-80 and ferulic acid. In the clarification assay, endo-xylanase successfully clarified the juices of mango (51.11%), banana (9.99%) and tangerine (8.54%). Furthermore, the enzyme also hydrolysed all fruit peel wastes that were tested. In summary, A. japonicus endo-xylanase showed potential for applications in fruit juice clarification and in the treatment of fruit peel wastes, and it is a good candidate for the food industry due to its wide pH stability under acidic conditions. MenosThe endo-xylanase from Aspergillus japonicus (UFMS 48.136) was purified in a single step using carboximethylcellulose chromatographic column and applied in fruit juice clarification process and fruit peel waste hydrolysis. This purification procedure resulted in 38.9-fold purification of endo-xylanase with 83.3% final yield. MALDITOF analysis confirmed the molecular mass of 32 kDa. The optimal purified endo-xylanase activity was at a range of pH from 5.0 to 6.0 and from 50 to 60 +-C, retaining more than 70% of its activity at all pH studied (3.0?8.0) for 24 h at room temperature. The A. japonicus endo-xylanolytic activity stimulation curve was assayed in the presence of different birchwood xylan concentrations (ranging from 0.02 to 0.5% w/v) and the endoxylanase activity presented a Vmax of 467.4 +- 30.38 μmol/min/mg, with a km of 2.59 +- 0.17 mg/mL, a kcat of 253.95 +- 16.51 s -1 and a kcat/km value of 98.05 +- 4.41 mL s -1 mg -1. The endo-xylanase was activated by Mn2þ (34.5%) and inhibited by Cu2þ (56.9%). The endo-xylanase was activated by β-mercaptoethanol, Triton X-100, Tween-20, Tween-80 and ferulic acid. In the clarification assay, endo-xylanase successfully clarified the juices of mango (51.11%), banana (9.99%) and tangerine (8.54%). Furthermore, the enzyme also hydrolysed all fruit peel wastes that were tested. In summary, A. japonicus endo-xylanase showed potential for applications in fruit juice clarification and in the treatment of fruit peel wastes, a... Mostrar Tudo |
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Palavras-Chave: |
Endo-xylanase; Fruit juice clarification; Purification Aspergillus sp. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/209484/1/Application-of-an-endo-xylanase.pdf
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Marc: |
LEADER 02404naa a2200253 a 4500
001 2119240
005 2020-01-23
008 2019 bl uuuu u00u1 u #d
100 1 $aSILVA, P. O. da
245 $aApplication of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.$h[electronic resource]
260 $c2019
520 $aThe endo-xylanase from Aspergillus japonicus (UFMS 48.136) was purified in a single step using carboximethylcellulose chromatographic column and applied in fruit juice clarification process and fruit peel waste hydrolysis. This purification procedure resulted in 38.9-fold purification of endo-xylanase with 83.3% final yield. MALDITOF analysis confirmed the molecular mass of 32 kDa. The optimal purified endo-xylanase activity was at a range of pH from 5.0 to 6.0 and from 50 to 60 +-C, retaining more than 70% of its activity at all pH studied (3.0?8.0) for 24 h at room temperature. The A. japonicus endo-xylanolytic activity stimulation curve was assayed in the presence of different birchwood xylan concentrations (ranging from 0.02 to 0.5% w/v) and the endoxylanase activity presented a Vmax of 467.4 +- 30.38 μmol/min/mg, with a km of 2.59 +- 0.17 mg/mL, a kcat of 253.95 +- 16.51 s -1 and a kcat/km value of 98.05 +- 4.41 mL s -1 mg -1. The endo-xylanase was activated by Mn2þ (34.5%) and inhibited by Cu2þ (56.9%). The endo-xylanase was activated by β-mercaptoethanol, Triton X-100, Tween-20, Tween-80 and ferulic acid. In the clarification assay, endo-xylanase successfully clarified the juices of mango (51.11%), banana (9.99%) and tangerine (8.54%). Furthermore, the enzyme also hydrolysed all fruit peel wastes that were tested. In summary, A. japonicus endo-xylanase showed potential for applications in fruit juice clarification and in the treatment of fruit peel wastes, and it is a good candidate for the food industry due to its wide pH stability under acidic conditions.
653 $aEndo-xylanase
653 $aFruit juice clarification
653 $aPurification Aspergillus sp
700 1 $aGUIMARÃES, N. C. de A.
700 1 $aSERPA, J. D. M.
700 1 $aMASUI, D. C.
700 1 $aMARCHETTI, C. R.
700 1 $aVERBISCK, N. V.
700 1 $aZANOELO, F. F.
700 1 $aRULLER, R.
700 1 $aGIANNESI, G. C.
773 $tBiocatalysis and Agricultural Biotechnology$gv. 21, 2019.
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Registro original: |
Embrapa Gado de Corte (CNPGC) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Tabuleiros Costeiros. Para informações adicionais entre em contato com cpatc.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Tabuleiros Costeiros. |
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Data corrente: |
18/11/2008 |
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Data da última atualização: |
12/02/2009 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
TAQUEDA, G. S.; AZEVEDO, H. C. |
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Afiliação: |
Gustavo Santro Taqueda, (bolsista) Embrapa Tabuleiros Costeiros; Hymerson Costa Azevedo, Embrapa Tabuleiros Costeiros. |
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Título: |
Aumento da taxa de ovulação em ovinos Santa Inês determinada pela mutação FECGSL. (Projeto de Mestrado). |
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Ano de publicação: |
2008 |
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Fonte/Imprenta: |
In: ENCONTRO DE INICIAÇÃO CIENTÍFICA, 18; ENCONTRO DE PÓS-GRADUAÇÃO, 4., 2008, São Cristóvão. Anais... São Cristóvão: UFS, 2008. Biotecnologia. 1 CD-ROM. |
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Idioma: |
Português |
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Palavras-Chave: |
Ovono Santa Inês; Resumo. |
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Thesagro: |
Ovulação. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 00597naa a2200157 a 4500
001 1372320
005 2009-02-12
008 2008 bl uuuu u00u1 u #d
100 1 $aTAQUEDA, G. S.
245 $aAumento da taxa de ovulação em ovinos Santa Inês determinada pela mutação FECGSL. (Projeto de Mestrado).
260 $c2008
650 $aOvulação
653 $aOvono Santa Inês
653 $aResumo
700 1 $aAZEVEDO, H. C.
773 $tIn: ENCONTRO DE INICIAÇÃO CIENTÍFICA, 18; ENCONTRO DE PÓS-GRADUAÇÃO, 4., 2008, São Cristóvão. Anais... São Cristóvão: UFS, 2008. Biotecnologia. 1 CD-ROM.
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