Conformational stability of recombinant manganese superoxide dismutase from the filamentous fungus Trichoderma reesei
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
07/11/2013
07/11/2013
2012
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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 |
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 |