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Self-sustained n-Type Memory Transistor Devices Based on Natural Cellulose Paper Fibers
Rodrigo Martins,Luís Pereira,Pedro Barquinha,Nuno Correia,Gonçalo Gonçalves,Isabel Ferreira,Carlos Dias,Elvira Fortunato,N. Correia,M. Dionísio,M. Silva 한국정보디스플레이학회 2009 Journal of information display Vol.10 No.4
Reported herein is the architecture for a nonvolatile n-type memory paper field-effect transistor. The device was built via the hybrid integration of natural cellulose fibers (pine and eucalyptus fibers embedded in resin withionic additives), which act simultaneously as substrate and gate dielectric, using passive and active semiconductors, respectively, as well as amorphous indium zinc and gallium indium zinc oxides for the gate electrode and channel layer, respectively. This was complemented by the use of continuous patterned metal layers as source/drain electrodes.
Immobilization of commercial acid phosphatases from wheat germ and potato onto ion exchangers
Lima Frederico Alves,Martins Pedro Alves,Wilson Galvão de Morais Júnior,Ribeiro Eloízio Júlio,Guisán José Manuel,de Resende Miriam Maria 한국화학공학회 2023 Korean Journal of Chemical Engineering Vol.40 No.9
A very simple and fast immobilization technique based on ion exchange was investigated to improve the thermal stability of acid phosphatase from wheat germ and potato. Immobilization was not efficient for the DEAE-sepharose, and MANAE-agarose supports. On the other hand, Toyopearl DEAE-650s proved to be a promising support, with immobilization yield above 95% and recovery of activity above 85% for both enzymes. A second step was introduced in the immobilization protocol to improve the thermal stability of these biocatalysts. For this, oxidation and reduction of glycosidic chains of acid phosphatase were carried out, allowing the formation of aldehyde groups and subsequent interaction with the amine groups to further stabilize the different forms (free and immobilized). Both biocatalysts showed residual activity after 1 hour of inactivation at the temperature of 60 °C, a fact not observed for the free enzyme. The wheat germ acid phosphatase derivative was the most stable, with residual activity of 66.7% for the only immobilized derivative and 76.2% for the oxidized/reduced derivative. Also, the derivatives prepared by ion exchange adsorption on Toyopearl (TOYO), followed by oxidation/reduction and intramolecular crosslinking, were approximately 15 and 41 times more stable than the free enzyme from wheat germ.