A Novel Member of GH16 Family Derived from Sugarcane Soil Metagenome
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1007/s12010-015-1743-7 http://hdl.handle.net/11449/167978 |
Resumo: | Glycoside hydrolases (GHs) are enzymes found in all living kingdoms that are involved in multiple physiological functions. Due to their multiple enzymatic activities, GHs are broadly applied in bioethanol, food, and paper industry. In order to increase the productivity of these industrial processes, a constant search for novel and efficient enzymes has been proved to be necessary. In this context, metagenomics is a powerful approach to achieve this demand. In the current study, we describe the discovery and characterization of a novel member of GH16 family derived from the sugarcane soil metagenome. The enzyme, named SCLam, has 286 amino acid residues and displays sequence homology and activity properties that resemble known laminarases. SCLam is active against barley beta-glucan, laminarin, and lichenan (72, 33, and 10 U mg−1, respectively). The optimal reaction conditions were identified as 40 °C and pH 6.5. The low-resolution structure was determined using the small-angle X-ray scattering technique, revealing that SCLam is a monomer in solution with a radius of gyration equal to 19.6 Å. To the best of our knowledge, SCLam is the first nonspecific (1,3/1,3:1,4)-β-d-glucan endohydrolase (EC 3.2.1.6) recovered by metagenomic approach to be characterized. |
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A Novel Member of GH16 Family Derived from Sugarcane Soil MetagenomeGH16LaminaraseMetagenomicsNonspecific (1,3/1,3:1,4)-β-d-glucan endohydrolaseGlycoside hydrolases (GHs) are enzymes found in all living kingdoms that are involved in multiple physiological functions. Due to their multiple enzymatic activities, GHs are broadly applied in bioethanol, food, and paper industry. In order to increase the productivity of these industrial processes, a constant search for novel and efficient enzymes has been proved to be necessary. In this context, metagenomics is a powerful approach to achieve this demand. In the current study, we describe the discovery and characterization of a novel member of GH16 family derived from the sugarcane soil metagenome. The enzyme, named SCLam, has 286 amino acid residues and displays sequence homology and activity properties that resemble known laminarases. SCLam is active against barley beta-glucan, laminarin, and lichenan (72, 33, and 10 U mg−1, respectively). The optimal reaction conditions were identified as 40 °C and pH 6.5. The low-resolution structure was determined using the small-angle X-ray scattering technique, revealing that SCLam is a monomer in solution with a radius of gyration equal to 19.6 Å. To the best of our knowledge, SCLam is the first nonspecific (1,3/1,3:1,4)-β-d-glucan endohydrolase (EC 3.2.1.6) recovered by metagenomic approach to be characterized.Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE) Centro Nacional de Pesquisa em Energia e Materiais (CNPEM)Laboratório Nacional de Biociências (LNBio) Centro Nacional de Pesquisa em Energia e Materiais (CNPEM)Instituto de Física de São Carlos Universidade de São PauloDepartamento de Física e Biofísica Instituto de Biociências Universidade Estadual Paulista (UNESP)Departamento de Física e Biofísica Instituto de Biociências Universidade Estadual Paulista (UNESP)Centro Nacional de Pesquisa em Energia e Materiais (CNPEM)Universidade de São Paulo (USP)Universidade Estadual Paulista (Unesp)Alvarez, Thabata MariaLiberato, Marcelo VizonáCairo, João Paulo L. FrancoPaixão, Douglas A. A.Campos, Bruna M.Ferreira, Marcel R. [UNESP]Almeida, Rodrigo F.Pereira, Isabela O.Bernardes, AmandaEmatsu, Gabriela C. G.Chinaglia, MarianaPolikarpov, Igorde Oliveira Neto, Mario [UNESP]Squina, Fabio Marcio2018-12-11T16:39:06Z2018-12-11T16:39:06Z2015-09-28info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article304-317application/pdfhttp://dx.doi.org/10.1007/s12010-015-1743-7Applied Biochemistry and Biotechnology, v. 177, n. 2, p. 304-317, 2015.1559-02910273-2289http://hdl.handle.net/11449/16797810.1007/s12010-015-1743-72-s2.0-849404525212-s2.0-84940452521.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengApplied Biochemistry and Biotechnology0,571info:eu-repo/semantics/openAccess2023-12-23T06:23:37Zoai:repositorio.unesp.br:11449/167978Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-12-23T06:23:37Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
A Novel Member of GH16 Family Derived from Sugarcane Soil Metagenome |
title |
A Novel Member of GH16 Family Derived from Sugarcane Soil Metagenome |
spellingShingle |
A Novel Member of GH16 Family Derived from Sugarcane Soil Metagenome Alvarez, Thabata Maria GH16 Laminarase Metagenomics Nonspecific (1,3/1,3:1,4)-β-d-glucan endohydrolase |
title_short |
A Novel Member of GH16 Family Derived from Sugarcane Soil Metagenome |
title_full |
A Novel Member of GH16 Family Derived from Sugarcane Soil Metagenome |
title_fullStr |
A Novel Member of GH16 Family Derived from Sugarcane Soil Metagenome |
title_full_unstemmed |
A Novel Member of GH16 Family Derived from Sugarcane Soil Metagenome |
title_sort |
A Novel Member of GH16 Family Derived from Sugarcane Soil Metagenome |
author |
Alvarez, Thabata Maria |
author_facet |
Alvarez, Thabata Maria Liberato, Marcelo Vizoná Cairo, João Paulo L. Franco Paixão, Douglas A. A. Campos, Bruna M. Ferreira, Marcel R. [UNESP] Almeida, Rodrigo F. Pereira, Isabela O. Bernardes, Amanda Ematsu, Gabriela C. G. Chinaglia, Mariana Polikarpov, Igor de Oliveira Neto, Mario [UNESP] Squina, Fabio Marcio |
author_role |
author |
author2 |
Liberato, Marcelo Vizoná Cairo, João Paulo L. Franco Paixão, Douglas A. A. Campos, Bruna M. Ferreira, Marcel R. [UNESP] Almeida, Rodrigo F. Pereira, Isabela O. Bernardes, Amanda Ematsu, Gabriela C. G. Chinaglia, Mariana Polikarpov, Igor de Oliveira Neto, Mario [UNESP] Squina, Fabio Marcio |
author2_role |
author author author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Centro Nacional de Pesquisa em Energia e Materiais (CNPEM) Universidade de São Paulo (USP) Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Alvarez, Thabata Maria Liberato, Marcelo Vizoná Cairo, João Paulo L. Franco Paixão, Douglas A. A. Campos, Bruna M. Ferreira, Marcel R. [UNESP] Almeida, Rodrigo F. Pereira, Isabela O. Bernardes, Amanda Ematsu, Gabriela C. G. Chinaglia, Mariana Polikarpov, Igor de Oliveira Neto, Mario [UNESP] Squina, Fabio Marcio |
dc.subject.por.fl_str_mv |
GH16 Laminarase Metagenomics Nonspecific (1,3/1,3:1,4)-β-d-glucan endohydrolase |
topic |
GH16 Laminarase Metagenomics Nonspecific (1,3/1,3:1,4)-β-d-glucan endohydrolase |
description |
Glycoside hydrolases (GHs) are enzymes found in all living kingdoms that are involved in multiple physiological functions. Due to their multiple enzymatic activities, GHs are broadly applied in bioethanol, food, and paper industry. In order to increase the productivity of these industrial processes, a constant search for novel and efficient enzymes has been proved to be necessary. In this context, metagenomics is a powerful approach to achieve this demand. In the current study, we describe the discovery and characterization of a novel member of GH16 family derived from the sugarcane soil metagenome. The enzyme, named SCLam, has 286 amino acid residues and displays sequence homology and activity properties that resemble known laminarases. SCLam is active against barley beta-glucan, laminarin, and lichenan (72, 33, and 10 U mg−1, respectively). The optimal reaction conditions were identified as 40 °C and pH 6.5. The low-resolution structure was determined using the small-angle X-ray scattering technique, revealing that SCLam is a monomer in solution with a radius of gyration equal to 19.6 Å. To the best of our knowledge, SCLam is the first nonspecific (1,3/1,3:1,4)-β-d-glucan endohydrolase (EC 3.2.1.6) recovered by metagenomic approach to be characterized. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-09-28 2018-12-11T16:39:06Z 2018-12-11T16:39:06Z |
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/s12010-015-1743-7 Applied Biochemistry and Biotechnology, v. 177, n. 2, p. 304-317, 2015. 1559-0291 0273-2289 http://hdl.handle.net/11449/167978 10.1007/s12010-015-1743-7 2-s2.0-84940452521 2-s2.0-84940452521.pdf |
url |
http://dx.doi.org/10.1007/s12010-015-1743-7 http://hdl.handle.net/11449/167978 |
identifier_str_mv |
Applied Biochemistry and Biotechnology, v. 177, n. 2, p. 304-317, 2015. 1559-0291 0273-2289 10.1007/s12010-015-1743-7 2-s2.0-84940452521 2-s2.0-84940452521.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Applied Biochemistry and Biotechnology 0,571 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
304-317 application/pdf |
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_ |
1797790089951051776 |