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        Glucose biofuel cells using bi-enzyme catalysts including glucose oxidase, horseradish peroxidase and terephthalaldehyde crosslinker

        Chung, Yongjin,Tannia, Daniel Chris,Kwon, Yongchai Elsevier 2018 CHEMICAL ENGINEERING JOURNAL -LAUSANNE- Vol.334 No.-

        <P><B>Abstract</B></P> <P>Biocatalysts consisting of bi-enzyme of glucose oxidase (GOx) and horseradish peroxidase (HRP) and terephthalaldehyde (TPA) as cross-linker ([(TPA/HRP/GOx)]/PEI/CNT) that have different GOx and HRP mass ratio are developed and their catalytic activity about glucose oxidation reaction and electrical performance evaluated via biofuel cell are characterized. To gain the optimal catalytic structure, current density peak of flavin adenine dinucleotide redox reaction, electron transfer rate, Michaelis-Menten constants, sensitivity and catalytic stability are measured. As a result, [(TPA/HRP/GOx)]/PEI/CNT whose HRP and GOx ratio is 2:5 is determined as the best catalyst. It is ascribed to superior catalytic activity of GOx and H<SUB>2</SUB>O<SUB>2</SUB> reduction reaction ability of HRP. Regarding electrical performance, polarization curves of enzymatic biofuel cells (EBCs) using the associated catalysts indicate that maximum power density (MPD) of EBC using [(TPA/HRP/GOx)]/PEI/CNT (HRP and GOx ratio of 2:5) is 2.0 ± 0.1 mW·cm<SUP>−2</SUP>, which is the highest of all the tested EBCs. Based on that, it is obvious that the optimal [(TPA/HRP/GOx)]/PEI/CNT induces improvements in catalytic activity and EBC performance due to proper removal of toxic H<SUB>2</SUB>O<SUB>2</SUB> molecules by HRP, excellent glucose reactivity by GOx and stable bonding of the catalytic structure by TPA.</P> <P><B>Highlights</B></P> <P> <UL> <LI> [(TPA/HRP/GOx)]/PEI/CNT catalyst is suggested as anodic catalyst of EBC. </LI> <LI> Optimal GOx and HRP mass ratio determines catalytic activity of the catalyst. </LI> <LI> TPA leads to stable bonding of the catalytic structure. </LI> <LI> There are effects of H<SUB>2</SUB>O<SUB>2</SUB> removal by HRP and excellent glucose reactivity by GOx. </LI> <LI> EBC employing [(TPA/HRP/GOx)]/PEI/CNT catalyst indicates excellent performance. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>

      • KCI등재

        Antioxidant Activity of Collagen Extracts Obtained from the Skin and Gills of Oreochromis sp.

        Jose Roberto Medina-Medrano,Tannia Alexandra Quin˜ones-Mun˜oz,Abel Arce-Ortı´z,Juan Gabriel Torruco-Uco,Ricardo Herna´ndez-Martı´nez,Manuel Alejandro Lizardi-Jime´nez,Elizabeth Varela-Santos 한국식품영양과학회 2019 Journal of medicinal food Vol.22 No.7

        Efforts aimed at reduction of fishing waste generated during the evisceration and filleting are scarce. The fishing waste is used in the production of low value-added products, such as flours or silages. It is important to visualize an alternative and profitable use of this waste, as it constitutes a serious environmental problem. This research determined the antioxidant properties of collagenous extracts of skin and galls of Oreochromis sp. The raw materials were characterized by proximal chemical analysis. Three treatments were applied to extract the collagen: salt-soluble collagen, acid-soluble collagen (ASC), and pepsin-hydrolyzed collagen (PHC). The collagenous fractions were hydrolyzed (0.1% pepsin). The recovered collagen yield and antioxidant activity were determined to hydrolyzed collagen (HC) and nonhydrolyzed collagen (NHC). The ASC skin showed the highest extraction yield (3.02%). For galls, only the PHC extraction was feasible (0.16%). Antioxidant analysis of NHC did not reveal radical scavenging activities. HC displayed a 2,2-diphenyl-1-picrylhydrazyl %RSA of 22.58 (ASC skin) and 10.34% (PHC galls), and a 2,2′-azino-bis[3-ethylbenzothiazoline-6-sulfonic acid] %RSA of 30.40% (PHC skin) and 29.43% (PHC galls), respectively. The ASC skin and PHC gall extracts exhibited 94.40% and 81.54% in ferric-reducing antioxidant power, and 43.63 and 38.08 μg ascorbic acid equivalents per milli liter for total antioxidant capacity, respectively. The collagen extracts showed %RSA and chelation of pro-oxidant metal ions. Different mechanism of antioxidant action was identified for the extracts: radical scavengers for HC and metal ion chelators for NHC. In conclusion, red tilapia skin collagen is recommended as an active ingredient of nutraceuticals, pharmaceuticals, or functional foods, for the identified bioactive properties.

      • SCISCIESCOPUS

        Biocatalyst including porous enzyme cluster composite immobilized by two-step crosslinking and its utilization as enzymatic biofuel cell

        Chung, Yongjin,Christwardana, Marcelinus,Tannia, Daniel Chris,Kim, Ki Jae,Kwon, Yongchai Elsevier Sequoia 2017 Journal of Power Sources Vol. No.

        <P><B>Abstract</B></P> <P>An enzyme cluster composite (TPA/GOx) formed from glucose oxidase (GOx) and terephthalaldehyde (TPA) that is coated onto polyethyleneimine (PEI) and carbon nanotubes (CNTs) is suggested as a new catalyst ([(TPA/GOx)/PEI]/CNT). In this catalyst, TPA promotes inter-GOx links by crosslinking to form a large and porous structure, and the TPA/GOx composite is again crosslinked with PEI/CNT to increase the amount of immobilized GOx. Such a two-step crosslinking (i) increases electron transfer because of electron delocalization by π conjugation and (ii) reduces GOx denaturation because of the formation of strong chemical bonds while its porosity facilitates mass transfer. With these features, an enzymatic biofuel cell (EBC) employing the new catalyst is fabricated and induces an excellent maximum power density (1.62 ± 0.08 mW cm<SUP>−2</SUP>), while the catalytic activity of the [(TPA/GOx)/PEI]/CNT catalyst is outstanding. This is clear evidence that the two-step crosslinking and porous structure caused by adoption of the TPA/GOx composite affect the performance enhancement of EBC.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Porous [TPA/GOx]/PEI/CNT catalyst is suggested by using two-step crosslinking. </LI> <LI> The catalyst increases electron transfer by electron delocalization by π conjugation. </LI> <LI> The catalyst curtails enzyme denaturation by strong chemical bonding. </LI> <LI> The catalyst induces superior EBC performance. </LI> <LI> Terephthalaldehyde (TPA) promotes inter-GOx links to form large and porous structure. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>

      • KCI등재

        Effects of the gold nanoparticles including different thiol functional groups on the performances of glucose-oxidase-based glucose sensing devices

        Marcelinus Christwardana,정용진,Daniel Chris Tannia,Yongchai Kwon 한국화학공학회 2018 Korean Journal of Chemical Engineering Vol.35 No.12

        Thiol-based self-assembled anchor linked to glucose oxidase (GOx) and gold nanoparticle (GNP) cluster is suggested to enhance the performance of glucose biosensor. By the adoption of thiol-based anchors, the activity of biocatalyst consisting of GOx, GNP, polyethyleneimine (PEI) and carbon nanotube (CNT) is improved because they play a crucial role in preventing the leaching out of GOx. They also promote electron collection and transfer, and this is due to a strong hydrophobic interaction between the active site of GOx and the aromatic ring of anchor, while the effect is optimized with the use of thiophenol anchor due to its simple configuration. Based on that, it is quantified that by the adoption of thiophenol as anchor, the current density of flavin adenine dinucleotide (FAD) redox reaction increases about 42%, electron transfer rate constant (ks) is 9.1±0.1 s1 and the value is 26% higher than that of catalyst that does not use the anchor structure.

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