Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4
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 UNESP |
Texto Completo: | http://dx.doi.org/10.1007/s12010-019-02973-8 http://hdl.handle.net/11449/190127 |
Resumo: | Xylanases are enzymes that act in the depolymerization of xylan and that can be used in the food industry, the paper industry, and for bioenergy, among other uses. In this context, particular emphasis is devoted to xylooligosaccharides (XOS) that act as prebiotics, which, under the action of probiotic microorganisms, are capable of positively modifying the intestinal microbiota. In this sense, searching for microbial xylanases stands out as a sustainable strategy for the production of prebiotics. To date, there have been no reports in the literature regarding the purification of native xylanase from Myceliophthora heterothallica F.2.1.4. In this study, a xylanase from this fungus was purified and characterized. The xylanase, with 27 kDa, showed maximum activity at pH 4.5 and 65–70 °C. It maintained more than 80% of its residual activity when exposed to (i) temperatures between 30 and 60 °C for 1 h and (ii) pH 5–10 for 24 h at 4 and 25 °C. These high tolerances to different pH and different temperatures are important properties that add value to this enzyme. The hydrolysates of this enzyme on beechwood xylan, analyzed by HPAE-PAD, were mostly xylobiose (X2) and xylotriose (X3). Hydrolysates were also quantified, being retrieved from 234.2 mg xylooligosaccharides/g of hydrolyzed xylan for 12 h. According to the products obtained from the xylan hydrolysis and its tolerance properties of the enzyme, it has demonstrated potential for application production of xylooligosaccharides for use as prebiotics. |
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Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4Fungal enzymePurificationXylanaseXylooligosaccharidesXylanases are enzymes that act in the depolymerization of xylan and that can be used in the food industry, the paper industry, and for bioenergy, among other uses. In this context, particular emphasis is devoted to xylooligosaccharides (XOS) that act as prebiotics, which, under the action of probiotic microorganisms, are capable of positively modifying the intestinal microbiota. In this sense, searching for microbial xylanases stands out as a sustainable strategy for the production of prebiotics. To date, there have been no reports in the literature regarding the purification of native xylanase from Myceliophthora heterothallica F.2.1.4. In this study, a xylanase from this fungus was purified and characterized. The xylanase, with 27 kDa, showed maximum activity at pH 4.5 and 65–70 °C. It maintained more than 80% of its residual activity when exposed to (i) temperatures between 30 and 60 °C for 1 h and (ii) pH 5–10 for 24 h at 4 and 25 °C. These high tolerances to different pH and different temperatures are important properties that add value to this enzyme. The hydrolysates of this enzyme on beechwood xylan, analyzed by HPAE-PAD, were mostly xylobiose (X2) and xylotriose (X3). Hydrolysates were also quantified, being retrieved from 234.2 mg xylooligosaccharides/g of hydrolyzed xylan for 12 h. According to the products obtained from the xylan hydrolysis and its tolerance properties of the enzyme, it has demonstrated potential for application production of xylooligosaccharides for use as prebiotics.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)São Paulo State University (Unesp) Institute of Biosciences Humanities and Exact Sciences, São José do Rio PretoSão Paulo State University (Unesp) Institute of Biosciences Humanities and Exact Sciences, São José do Rio PretoCAPES: 2018/2019CNPq: 426578/2016-3FAPESP: Process 2017/16482-5Universidade Estadual Paulista (Unesp)de Oliveira Simões, Lorena Caixeta [UNESP]da Silva, Ronivaldo Rodrigues [UNESP]de Oliveira Nascimento, Carlos Eduardo [UNESP]Boscolo, Maurício [UNESP]Gomes, Eleni [UNESP]da Silva, Roberto [UNESP]2019-10-06T17:03:14Z2019-10-06T17:03:14Z2019-08-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article991-1008http://dx.doi.org/10.1007/s12010-019-02973-8Applied Biochemistry and Biotechnology, v. 188, n. 4, p. 991-1008, 2019.1559-02910273-2289http://hdl.handle.net/11449/19012710.1007/s12010-019-02973-82-s2.0-850617380798880074921989984Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengApplied Biochemistry and Biotechnologyinfo:eu-repo/semantics/openAccess2021-10-23T16:30:44Zoai:repositorio.unesp.br:11449/190127Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:10:49.320840Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4 |
title |
Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4 |
spellingShingle |
Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4 de Oliveira Simões, Lorena Caixeta [UNESP] Fungal enzyme Purification Xylanase Xylooligosaccharides |
title_short |
Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4 |
title_full |
Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4 |
title_fullStr |
Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4 |
title_full_unstemmed |
Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4 |
title_sort |
Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4 |
author |
de Oliveira Simões, Lorena Caixeta [UNESP] |
author_facet |
de Oliveira Simões, Lorena Caixeta [UNESP] da Silva, Ronivaldo Rodrigues [UNESP] de Oliveira Nascimento, Carlos Eduardo [UNESP] Boscolo, Maurício [UNESP] Gomes, Eleni [UNESP] da Silva, Roberto [UNESP] |
author_role |
author |
author2 |
da Silva, Ronivaldo Rodrigues [UNESP] de Oliveira Nascimento, Carlos Eduardo [UNESP] Boscolo, Maurício [UNESP] Gomes, Eleni [UNESP] da Silva, Roberto [UNESP] |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
de Oliveira Simões, Lorena Caixeta [UNESP] da Silva, Ronivaldo Rodrigues [UNESP] de Oliveira Nascimento, Carlos Eduardo [UNESP] Boscolo, Maurício [UNESP] Gomes, Eleni [UNESP] da Silva, Roberto [UNESP] |
dc.subject.por.fl_str_mv |
Fungal enzyme Purification Xylanase Xylooligosaccharides |
topic |
Fungal enzyme Purification Xylanase Xylooligosaccharides |
description |
Xylanases are enzymes that act in the depolymerization of xylan and that can be used in the food industry, the paper industry, and for bioenergy, among other uses. In this context, particular emphasis is devoted to xylooligosaccharides (XOS) that act as prebiotics, which, under the action of probiotic microorganisms, are capable of positively modifying the intestinal microbiota. In this sense, searching for microbial xylanases stands out as a sustainable strategy for the production of prebiotics. To date, there have been no reports in the literature regarding the purification of native xylanase from Myceliophthora heterothallica F.2.1.4. In this study, a xylanase from this fungus was purified and characterized. The xylanase, with 27 kDa, showed maximum activity at pH 4.5 and 65–70 °C. It maintained more than 80% of its residual activity when exposed to (i) temperatures between 30 and 60 °C for 1 h and (ii) pH 5–10 for 24 h at 4 and 25 °C. These high tolerances to different pH and different temperatures are important properties that add value to this enzyme. The hydrolysates of this enzyme on beechwood xylan, analyzed by HPAE-PAD, were mostly xylobiose (X2) and xylotriose (X3). Hydrolysates were also quantified, being retrieved from 234.2 mg xylooligosaccharides/g of hydrolyzed xylan for 12 h. According to the products obtained from the xylan hydrolysis and its tolerance properties of the enzyme, it has demonstrated potential for application production of xylooligosaccharides for use as prebiotics. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-10-06T17:03:14Z 2019-10-06T17:03:14Z 2019-08-15 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1007/s12010-019-02973-8 Applied Biochemistry and Biotechnology, v. 188, n. 4, p. 991-1008, 2019. 1559-0291 0273-2289 http://hdl.handle.net/11449/190127 10.1007/s12010-019-02973-8 2-s2.0-85061738079 8880074921989984 |
url |
http://dx.doi.org/10.1007/s12010-019-02973-8 http://hdl.handle.net/11449/190127 |
identifier_str_mv |
Applied Biochemistry and Biotechnology, v. 188, n. 4, p. 991-1008, 2019. 1559-0291 0273-2289 10.1007/s12010-019-02973-8 2-s2.0-85061738079 8880074921989984 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Applied Biochemistry and Biotechnology |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
991-1008 |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128614779060224 |