Cloning, Identification and Isolation a Glucose Oxidase Gene (GOX) from Penicillium funiculosum

Glucose oxidase (β-D-glucose: oxygen 1-oxidoreductase) catalyzes the oxidation of β-D-glucose to gluconic acid، by utilizing molecular oxygen as an electron acceptor with simultaneous production of hydrogen peroxide. Glucose oxidase has been purified from a range of different fungal sources، mainly from the genus Aspergillus and Penicillium and has wide applications in chemical، pharmaceutical، food، biotechnology and other industries. In this study، a glucose oxidase (GOX) -encoding gene was isolated from Penicillium funiculosum by polymerase chain reaction (PCR) technique and then was cloned into a pUC19 plasmid. Consequently، molecular structure، biochemical and phylogenetic characteristics were analyzed. Nucleotide sequence of the gene، called PfGOX، revealed 1818 bp long، encoding a protein of 605 amino acid residues. The calculated molecular mass and the predicted isoelectric point of the deduced polypeptide were 65. 79 kDa and 4. 50، respectively. Analysis of secondary and three dimensional structures of the deduced polypeptide sequence for PfGOX was shown that PfGOX is similar to those of previously reported glucose oxidase proteins from other fungi. The deduced protein sequence was indicated a high similarity to glucose oxidases isolated from fungi such as Penicillium amagasakiense، Talaromyces flavus، Talaromyces stipitatus، and Talaromyces variabilis. Phylogenetic study was also demonstrated that PfGOX gene belongs to the subgroup IA of fungous glucose oxidases