جستجوی مقالات مرتبط با کلیدواژه "گلوکز اکسیداز" در نشریات گروه "علوم پایه"

Multilayer nanometer substrates based on graphite have emerged as a new field in the design and manufacture of biocatalysts. Layered and self-assembled Nano surfaces can provide a significant accessible surface for the immobilization of drugs, biological systems, and active enzymes and also can be used for the detection of biomarkers. In this study, a new bioelectrode was fabricated by self-assembling a porous graphene pattern with a G-rich polymer (GRP). The highly hydrophobic porous graphene was functionalized with a guanine (G) rich polymer to incorporate glucose oxidase (GOx). Graphene sheet dispersed in water with guanine (G) rich polymer. The electrochemical response of the bioelectrode to glucose was studied as a model for bioelectrocatalysis. The bioelectrode displayed a linear response to glucose concentration ranging from 0.2 to 2 mM, with a detection limit of 0.086 µM and 0.092 µA/µM/cm2 sensitivity. This study illustrates the potential of porous graphene for the construction of bioelectronics interfaces for the fabrication of electrochemical bio-devices.

Glucose oxidase (GOX) is considered a commercial enzyme in the medicine, pharmaceutical, and food industries. Optimization of the fermentation medium and conditions is important to increase heterologous GOX production. The current study aimed to optimize GOX production in a ‎recombinant strain of Yarrowia lipolytica via statistical techniques.

Response surface methodology (RSM) as a statistical technique for the design of the experiment was used for the optimization of recombinant GOX production by Y. lipolytica. Then, the optimized conditions were used for the production of GOX in bioreactor cultivation.

GOX production was increased up to 570 U/L after optimization of the medium in flask culture which is 2 times more than the non-optimized medium. In the bioreactor culture using optimized medium containing glucose and sucrose as carbon sources, GOX production was reached 720 and 730 U/L after two and six days, respectively.

Results of the study provided valuable information about the statistical optimization of bioprocess development for the production of heterologous protein in Y. lipolytica.

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