Biochemical characterization, thermal stability, and partial sequence of a novel exo-polygalacturonase from the thermophilic fungus rhizomucor pusillus a13.36 obtained by submerged cultivation

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorTrindade, Lucas Vinícius-
Autor(es): dc.creatorDesagiacomo, Carla-
Autor(es): dc.creatorPolizeli, Maria De Lourdes Teixeira De Moraes-
Autor(es): dc.creatorDamasio, André Ricardo De Lima-
Autor(es): dc.creatorLima, Aline Margarete Furuyama-
Autor(es): dc.creatorGomes, Eleni-
Autor(es): dc.creatorBonilla-Rodriguez, Gustavo Orlando-
Data de aceite: dc.date.accessioned2021-03-11T00:53:57Z-
Data de disponibilização: dc.date.available2021-03-11T00:53:57Z-
Data de envio: dc.date.issued2018-12-11-
Data de envio: dc.date.issued2018-12-11-
Data de envio: dc.date.issued2016-01-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1155/2016/8653583-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/178483-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/178483-
Descrição: dc.descriptionThis work reports the production of an exo-polygalacturonase (exo-PG) by Rhizomucor pusillus A13.36 in submerged cultivation (SmC) in a shaker at 45°C for 96 h. A single pectinase was found and purified in order to analyze its thermal stability, by salt precipitation and hydrophobic interaction chromatography. The pectinase has an estimated Mw of approximately 43.5-47 kDa and optimum pH of 4.0 but is stable in pH ranging from 3.5 to 9.5 and has an optimum temperature of 61°C. It presents thermal stability between 30 and 60°C, has 70% activation in the presence of Ca2+, and was tested using citrus pectin with a degree of methyl esterification (DE) of 26%. Ea(d) for irreversible denaturation was 125.5 kJ/mol with positive variations of entropy and enthalpy for that and ΔG(d) values were around 50 kJ/mol. The hydrolysis of polygalacturonate was analyzed by capillary electrophoresis which displayed a pattern of sequential hydrolysis (exo). The partial identification of the primary sequence was done by MS MALDI-TOF and a comparison with data banks showed the highest identity of the sequenced fragments of exo-PG from R. pusillus with an exo-pectinase from Aspergillus fumigatus. Pectin hydrolysis showed a sigmoidal curve for the Michaelis-Menten plot.-
Idioma: dc.languageen-
Relação: dc.relationBioMed Research International-
Relação: dc.relation0,935-
Relação: dc.relation0,935-
Direitos: dc.rightsopenAccess-
Título: dc.titleBiochemical characterization, thermal stability, and partial sequence of a novel exo-polygalacturonase from the thermophilic fungus rhizomucor pusillus a13.36 obtained by submerged cultivation-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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