Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.

Detalhes bibliográficos
Autor(a) principal: SILVA, P. O. da
Data de Publicação: 2019
Outros Autores: 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.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
Texto Completo: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1119240
Resumo: 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.
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spelling Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.Endo-xylanasePurification Aspergillus spFruit juice clarificationThe 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.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.SILVA, P. O. daGUIMARÃES, 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.2020-01-23T18:06:54Z2020-01-23T18:06:54Z2020-01-2320192020-01-23T18:06:54Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleBiocatalysis and Agricultural Biotechnology, v. 21, 2019.http://www.alice.cnptia.embrapa.br/alice/handle/doc/1119240enginfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)instacron:EMBRAPA2020-01-23T18:07:01Zoai:www.alice.cnptia.embrapa.br:doc/1119240Repositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestopendoar:21542020-01-23T18:07:01falseRepositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestcg-riaa@embrapa.bropendoar:21542020-01-23T18:07:01Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)false
dc.title.none.fl_str_mv Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.
title Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.
spellingShingle Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.
SILVA, P. O. da
Endo-xylanase
Purification Aspergillus sp
Fruit juice clarification
title_short Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.
title_full Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.
title_fullStr Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.
title_full_unstemmed Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.
title_sort Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.
author SILVA, P. O. da
author_facet 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.
author_role author
author2 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.
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv 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.
dc.contributor.author.fl_str_mv 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.
dc.subject.por.fl_str_mv Endo-xylanase
Purification Aspergillus sp
Fruit juice clarification
topic Endo-xylanase
Purification Aspergillus sp
Fruit juice clarification
description 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.
publishDate 2019
dc.date.none.fl_str_mv 2019
2020-01-23T18:06:54Z
2020-01-23T18:06:54Z
2020-01-23
2020-01-23T18:06:54Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv Biocatalysis and Agricultural Biotechnology, v. 21, 2019.
http://www.alice.cnptia.embrapa.br/alice/handle/doc/1119240
identifier_str_mv Biocatalysis and Agricultural Biotechnology, v. 21, 2019.
url http://www.alice.cnptia.embrapa.br/alice/handle/doc/1119240
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
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instname_str Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
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reponame_str Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
collection Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
repository.name.fl_str_mv Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
repository.mail.fl_str_mv cg-riaa@embrapa.br
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