Bioelectrochemical study of the deglycosylated glucose oxidase enzyme for application in biofuel cells

• Grant number: 13/19908-2
• Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
• Start date until: December 01, 2013
• End date until: July 31, 2017
• Field of knowledge: Physical Sciences and Mathematics - Chemistry - Physical-Chemistry
• Principal Investigator: Frank Nelson Crespilho
• Grantee: Andressa Ribeiro Pereira
• Host Institution: Instituto de Química de São Carlos (IQSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil

Abstract

The Enzyme Glucose Oxidase (GOx) obtained from Aspergillus niger is one dimeric flavoprotein with approximately 160 kDa. This enzyme is responsible for catalytic oxidation of ²-D-glucose to D-glucono-´-lactona and hydrogen peroxide, utilizing the molecular oxygen as electron acceptor. Each monomer has one cofactor Flavine Adenine Dinucleotide (FAD) electrostatically bound to the protein structure. The GOx has high chemical stability and high specificity with glucose, arousing great interest to development biosensors and bioanodes for biofuel cells. Achieve the Direct Electron Transfer (DET) between active center of the enzyme and the electrode is very important to developing biodevices. The DET has been observed in redox proteins, when the active center is close to the protein surface, however, for GOx, the cofactor FAD is to deeply in the enzyme structure, which cause some difficulty the DET between the active center and the electrode surface. To facilitate this DET, it has been used glycoproteins deglycosylation, which decreases the distance between the enzymatic cofactor and the electrode surface, because this procedure breaks some glycans in the protein structure, allowing increasing the faradaic currents in the glucose oxidation, improving the performance of bioanodes in biofuel cells. In this context, this work has the goal to study the catalytic processes and the DET of deglycosylated GOx (dGOx) in flexible fiber of carbon to application in biofuel cells. For this, it will be utilize the trifluormethanesulfonic acid (TFMS) in chemical route and the enzymes ±-mannosidase e endoglycosidase H in enzymatic route of deglycosylation. We also study the processes of dGOx, immobilizing the enzyme, by adsorption, in glassy carbon electrode and in flexible fibers of carbon. (AU)

Scientific publications

(4)

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

PEREIRA, ANDRESSA R.; DE SOUZA, JOAO C. P.; GONCALVES, ANDRESSA D.; PAGNONCELLI, KAMILA C.; CRESPILHO, FRANK N.. Bioelectrooxidation of Ethanol Using NAD-Dependent Alcohol Dehydrogenase on Oxidized Flexible Carbon Fiber Arrays. Journal of the Brazilian Chemical Society, v. 28, n. 9, p. 1698-1707, SEP 2017. (15/16672-3, 13/14262-7, 13/19908-2)

PAGNONCELLI, KAMILA C.; PEREIRA, ANDRESSA R.; SEDENHO, GRAZIELA C.; BERTAGLIA, THIAGO; CRESPILHO, FRANK N.. Ethanol generation, oxidation and energy production in a cooperative bioelectrochemical system. BIOELECTROCHEMISTRY, v. 122, p. 11-25, AUG 2018. (15/16672-3, 13/14262-7, 13/19908-2, 15/22973-6)

PEREIRA, ANDRESSA R.; LUZ, ROBERTO A. S.; LIMA, FILIPE C. D. A.; CRESPILHO, FRANK N.. Protein Oligomerization Based on Bronsted Acid Reaction. ACS CATALYSIS, v. 7, n. 4, p. 3082-3088, APR 2017. (15/16672-3, 13/19908-2, 13/14262-7)

PEREIRA, ANDRESSA R.; DE SOUZA, JOAO C. P.; GONCALVES, ANDRESSA D.; PAGNONCELLI, KAMILA C.; CRESPILHO, FRANK N.. Bioelectrooxidation of Ethanol Using NAD-Dependent Alcohol Dehydrogenase on Oxidized Flexible Carbon Fiber Arrays. Journal of the Brazilian Chemical Society, v. 28, n. 9, p. 10-pg., 2017-09-01. (13/14262-7, 13/19908-2, 15/16672-3)

Academic Publications

(References retrieved automatically from State of São Paulo Research Institutions)

PEREIRA, Andressa Ribeiro. Oligomerization of glucose oxidase by using Brønsted acids for the application in bioelectrochemistry. 2017. Doctoral Thesis - Universidade de São Paulo (USP). Instituto de Química de São Carlos (IQSC/BT) São Carlos.