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A new β-glucosidase gene from the zygomycete fungus Rhizomucor miehei

Takó, Miklós, Tóth, Adél, Nagy, László G., Krisch, Judit, Vágvölgyi, Csaba, Papp, Tamás
Antonie van Leeuwenhoek 2010 v.97 no.1 pp. 1-10
Mucor, proteins, Rhizomucor miehei, plasmids, amino acids, active sites, introns, sequence homology, beta-glucosidase, fungi
In this study, a β-glucosidase coding gene (bgl) of the zygomycete fungus Rhizomucor miehei has been cloned and characterized. The gene comprises a total of 2,826 bp including the coding sequence of a 717 amino acids length putative protein and 10 introns dispersed in the whole coding region. The putative N-and C-terminal catalytic domains (aa 68 to aa 274 and aa 358-601, respectively) were identified; the two domains are connected with a 84-amino-acids linker. The catalytic region showed an extensive sequence homology with other fungal β-glucosidases classified as family 3 glycoside hydrolases. The isolated Rhizomucor gene was expressed in the related fungus Mucor circinelloides. Transformant Mucor strains maintained the introduced plasmid in an autoreplicative manner and showed significantly higher cellobiase activity than the recipient strain.