Produção Nacional
Revisado por pares
Cloning, characterization and heterologous expression of the first Penicillium echinulatum cellulase gene
2009; Oxford University Press; Volume: 108; Issue: 4 Linguagem: Inglês
10.1111/j.1365-2672.2009.04528.x
ISSN1365-2672
AutoresMarciano Régis Rubini, Aldo José Pinheiro Dillon, Cynthia Maria Kyaw, Fabrícia Paula de Faria, Márcio José Poças-Fonseca, Ildinete Silva-Pereira,
Tópico(s)Fungal and yeast genetics research
ResumoPenicillium echinulatum is effective for bioconversion processes. However, nothing is known about the molecular biology of its cellulolytic system. We describe for the first time the isolation, cloning and expression of a P. echinulatum cellulase cDNA (Pe-egl1) encoding a putative endoglucanase.Pe-egl1 cDNA was identified from random sequencing of a P. echinulatum cDNA library. The deduced EGL1 protein possibly belongs to the glycosyl hydrolase family 5A, with 387 amino acid residues and strong similarity with other fungal endoglucanases. The cDNA was heterologously expressed in Pichia pastoris. The recombinant EGL1 secreted by a Pic. pastoris recombinant strain revealed the characteristics of particular interest: an optimal activity over a broad pH range (5.0-9.0), and an optimal temperature of 60 degrees C. The recombinant EGL1 also showed high thermostability (84% of residual activity after 1 h of pre-incubation at 70 degrees C). Calcium exerted a strong stimulatory effect over EGL1 activity.Altogether, these results point to the potential application of this P. echinulatum endoglucanase in cellulose processing industries, particularly the textile one because of its biochemical properties.The characterization and heterologous expression of the first P. echinulatun cDNA inaugurates the exploitation of this potential industrial micro-organism.
Referência(s)