Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima

Background: Chitinases are widely distributed enzymes that perform the biotransformation of chitin, one of the most abundant polysaccharides on the biosphere, into useful value-added chitooligosaccharides (COS) with a wide variety of biotechnological applications in food, health, and agricultural fi...

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Detalles Bibliográficos
Autores: Minguet Lobato, Marina, Cervantes, Fadia V., Míguez Rodríguez, Noa, Plou, Francisco Jose, Fernández Lobato, María
Tipo de recurso: artículo
Fecha de publicación:2024
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/716947
Acceso en línea:http://hdl.handle.net/10486/716947
https://dx.doi.org/10.1186/s12934-024-02300-9
Access Level:acceso abierto
Palabra clave:Biotransformation
GH18
chitin
chitin wastes
chitinase
chitooligosaccharides
chitosan
mestchnikowia
Biología y Biomedicina / Biología
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spelling Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrimaMinguet Lobato, MarinaCervantes, Fadia V.Míguez Rodríguez, NoaPlou, Francisco JoseFernández Lobato, MaríaBiotransformationGH18chitinchitin wasteschitinasechitooligosaccharideschitosanmestchnikowiaBiología y Biomedicina / BiologíaBackground: Chitinases are widely distributed enzymes that perform the biotransformation of chitin, one of the most abundant polysaccharides on the biosphere, into useful value-added chitooligosaccharides (COS) with a wide variety of biotechnological applications in food, health, and agricultural fields. One of the most important group of enzymes involved in the degradation of chitin comprises the glycoside hydrolase family 18 (GH18), which harbours endo- and exo-enzymes that act synergistically to depolymerize chitin. The secretion of a chitinase activity from the ubiquitous yeast Mestchnikowia pulcherrima and their involvement in the post-harvest biological control of fungal pathogens was previously reported. Results: Three new chitinases from M. pulcherrima, MpChit35, MpChit38 and MpChit41, were molecularly characterized and extracellularly expressed in Pichia pastoris to about 91, 90 and 71 mU ml− 1, respectively. The three enzymes hydrolysed colloidal chitin with optimal activity at 45 ºC and pH 4.0-4.5, increased 2-times their activities using 1 mM of Mn2+ and hydrolysed different types of commercial chitosan. The partial separation and characterization of the complex COS mixtures produced from the hydrolysis of chitin and chitosan were achieved by a new anionic chromatography HPAEC-PAD method and mass spectrometry assays. An overview of the predicted structures of these proteins and their catalytic modes of action were also presented. Depicted their high sequence and structural homology, MpChit35 acted as an exo-chitinase producing di-acetyl-chitobiose from chitin while MpChit38 and MpChit41 both acted as endo-chitinases producing tri-acetyl-chitotriose as main final product. Conclusions: Three new chitinases from the yeast M. pulcherrima were molecularly characterized and their enzymatic and structural characteristics analysed. These enzymes transformed chitinous materials to fully and partially acetylated COS through different modes of splitting, which make them interesting biocatalysts for deeper structural-function studies on the challenging enzymatic conversion of chitinOpen Access funding provided thanks to the CRUE-CSIC agreement with Springer Nature. This work was supported the Spanish Ministry of Economy and Competitiveness and of Science and Innovation (PID2019-105838RB-C31/-C32; TED2021-129288B-C21/-C22; PID2022-136367OB-C31/-C32) and Fundación Ramón Areces (XIX Call of Research Grants in Life and Material Sciences). We thank Fundación Ramón Areces for an Institutional grant to CBMSO. The first author is supported by grant PRE2020-092330 from the Spanish Ministry of Science and InnovationBioMed Central LtdDepartamento de Biología MolecularFacultad de Ciencias20242024-01-20research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10486/716947https://dx.doi.org/10.1186/s12934-024-02300-9reponame:Biblos-e Archivo. Repositorio Institucional de la UAMinstname:Universidad Autónoma de MadridInglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:repositorio.uam.es:10486/7169472026-06-23T12:46:27Z
dc.title.none.fl_str_mv Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima
title Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima
spellingShingle Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima
Minguet Lobato, Marina
Biotransformation
GH18
chitin
chitin wastes
chitinase
chitooligosaccharides
chitosan
mestchnikowia
Biología y Biomedicina / Biología
title_short Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima
title_full Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima
title_fullStr Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima
title_full_unstemmed Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima
title_sort Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima
dc.creator.none.fl_str_mv Minguet Lobato, Marina
Cervantes, Fadia V.
Míguez Rodríguez, Noa
Plou, Francisco Jose
Fernández Lobato, María
author Minguet Lobato, Marina
author_facet Minguet Lobato, Marina
Cervantes, Fadia V.
Míguez Rodríguez, Noa
Plou, Francisco Jose
Fernández Lobato, María
author_role author
author2 Cervantes, Fadia V.
Míguez Rodríguez, Noa
Plou, Francisco Jose
Fernández Lobato, María
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Departamento de Biología Molecular
Facultad de Ciencias
dc.subject.none.fl_str_mv Biotransformation
GH18
chitin
chitin wastes
chitinase
chitooligosaccharides
chitosan
mestchnikowia
Biología y Biomedicina / Biología
topic Biotransformation
GH18
chitin
chitin wastes
chitinase
chitooligosaccharides
chitosan
mestchnikowia
Biología y Biomedicina / Biología
description Background: Chitinases are widely distributed enzymes that perform the biotransformation of chitin, one of the most abundant polysaccharides on the biosphere, into useful value-added chitooligosaccharides (COS) with a wide variety of biotechnological applications in food, health, and agricultural fields. One of the most important group of enzymes involved in the degradation of chitin comprises the glycoside hydrolase family 18 (GH18), which harbours endo- and exo-enzymes that act synergistically to depolymerize chitin. The secretion of a chitinase activity from the ubiquitous yeast Mestchnikowia pulcherrima and their involvement in the post-harvest biological control of fungal pathogens was previously reported. Results: Three new chitinases from M. pulcherrima, MpChit35, MpChit38 and MpChit41, were molecularly characterized and extracellularly expressed in Pichia pastoris to about 91, 90 and 71 mU ml− 1, respectively. The three enzymes hydrolysed colloidal chitin with optimal activity at 45 ºC and pH 4.0-4.5, increased 2-times their activities using 1 mM of Mn2+ and hydrolysed different types of commercial chitosan. The partial separation and characterization of the complex COS mixtures produced from the hydrolysis of chitin and chitosan were achieved by a new anionic chromatography HPAEC-PAD method and mass spectrometry assays. An overview of the predicted structures of these proteins and their catalytic modes of action were also presented. Depicted their high sequence and structural homology, MpChit35 acted as an exo-chitinase producing di-acetyl-chitobiose from chitin while MpChit38 and MpChit41 both acted as endo-chitinases producing tri-acetyl-chitotriose as main final product. Conclusions: Three new chitinases from the yeast M. pulcherrima were molecularly characterized and their enzymatic and structural characteristics analysed. These enzymes transformed chitinous materials to fully and partially acetylated COS through different modes of splitting, which make them interesting biocatalysts for deeper structural-function studies on the challenging enzymatic conversion of chitin
publishDate 2024
dc.date.none.fl_str_mv 2024
2024-01-20
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10486/716947
https://dx.doi.org/10.1186/s12934-024-02300-9
url http://hdl.handle.net/10486/716947
https://dx.doi.org/10.1186/s12934-024-02300-9
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv BioMed Central Ltd
publisher.none.fl_str_mv BioMed Central Ltd
dc.source.none.fl_str_mv reponame:Biblos-e Archivo. Repositorio Institucional de la UAM
instname:Universidad Autónoma de Madrid
instname_str Universidad Autónoma de Madrid
reponame_str Biblos-e Archivo. Repositorio Institucional de la UAM
collection Biblos-e Archivo. Repositorio Institucional de la UAM
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.81155

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