Conformational stability of recombinant manganese superoxide dismutase from the filamentous fungus Trichoderma reesei


Autoria(s): Alcalde, Felipe Santiago Chambergo; Valencia, Estela Y.; Ferreira Júnior, José Ribamar dos Santos; Camilo, Cesar M.; Campana, Patricia Targon
Contribuinte(s)

UNIVERSIDADE DE SÃO PAULO

Data(s)

07/11/2013

07/11/2013

2012

Resumo

Superoxide dismutases (SODS; EC 1.15.1.1) are part of the antioxidant system of aerobic organisms and are used as a defense against oxidative injury caused by reactive oxygen species (ROS). The cloning and sequencing of the 788-bp genomic DNA from Trichoderma reesei strain QM9414 (anamorph of Hypocrea jecorina) revealed an open reading frame encoding a protein of 212 amino acid residues, with 65-90% similarity to manganese superoxide dismutase from other filamentous fungi. The TrMnSOD was purified and shown to be stable from 20 to 90 degrees C for 1 h at pH from 8 to 11.5, while maintaining its biological activity. (C) 2011 Elsevier B.V. All rights reserved.

Fundacao de Amparo Pesquisa do Estado de Sao Paulo, FAPESP, Brazil [2007/50567-6]

Fundacao de Amparo Pesquisa do Estado de Sao Paulo (FAPESP), Brazil

Identificador

International Journal of Biological Macromolecules, Amsterdam, v. 50, n. 1, supl. 1, Part 2, pp. 19-24, 36892, 2012

0141-8130

http://www.producao.usp.br/handle/BDPI/42800

10.1016/j.ijbiomac.2011.09.015

http://dx.doi.org/10.1016/j.ijbiomac.2011.09.015

Idioma(s)

eng

Publicador

Elsevier Science BV

Amsterdam

Relação

International Journal of Biological Macromolecules

Direitos

closedAccess

Copyright ELSEVIER SCIENCE BV

Palavras-Chave #Trichoderma reesei #Superoxide dismutase #Circular dichroism #Thermal stability #PH stability #Protein secondary structure #Aspergillus-fumigatus #Gene-expression #Circular-dichroism #Hypocrea-jecorina #Purification #Sequence #Biodiversity #Mechanism #Glucose #Biochemistry & Molecular Biology
Tipo

article

original article

publishedVersion