Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4

Detalhes bibliográficos
Autor(a) principal: de Oliveira Simões, Lorena Caixeta [UNESP]
Data de Publicação: 2019
Outros Autores: da Silva, Ronivaldo Rodrigues [UNESP], de Oliveira Nascimento, Carlos Eduardo [UNESP], Boscolo, Maurício [UNESP], Gomes, Eleni [UNESP], da Silva, Roberto [UNESP]
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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spelling 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
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