Application of an endo-xylanase from Aspergillus japonicus in the fruit juice clarification and fruit peel waste hydrolysis.
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , , , , |
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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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 |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa) instacron:EMBRAPA |
instname_str |
Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
instacron_str |
EMBRAPA |
institution |
EMBRAPA |
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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1794503489019183104 |