Yazar "Baleviciute, I." seçeneğine göre listele

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    Conducting and Electrochemically Generated Polymers in Sensor Design (Mini Review)
    (ELSEVIER SCIENCE BV, 2012) Ramanavicius, A.; Oztekin, Y.; Balevicius, Z.; Kausaite-Mikstimiene, A.; Krikstolaityte, V.; Baleviciute, I.; Ratautaite, V.
    Various nanotechnological methods and high number of nanostructured materials including polymer nanocomposites (PNCs) become extremely important in sensor and biosensor technology. Conducting polymers as artificial versatile materials seem very suitable for the development of various analyte-recognizing parts of sensors and biosensors. This contribution is reviewing major fabrication methods of conducting polymer-based nanocomposites for biosensorics. Experience of authors in application of various electrochemically generated polymers in design of biosensors is presented. The influence of fabrication method on sensor characteristics is overviewed. Major types of biosensors based on conducting polymers including catalytic biosensors, DNA-sensors, immunosensors and molecularly imprinted polymer-based affinity sensors is discussed. Conducting and electrochemically generated polymers that are mostly used in sensor design are presented. (C) 2012 Elsevier Ltd....Selection and/or peer-review under responsibility of the Symposium Cracoviense Sp. z.o.o.
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    Fluorescence study of glucose oxidase self-encapsulated within polypyrrole
    (ELSEVIER SCIENCE SA, 2012) Ramanavicius, A.; Ryskevic, N.; Kausaite-Minkstimiene, A.; Bubniene, U.; Baleviciute, I.; Oztekin, Y.; Ramanaviciene, A.
    Glucose oxidase self-encapsulation within polypyrrole was achieved and this process was monitored by the registration of flavin adenine dinucleotide autofluorescence spectra at different periods. The fluorescence of non-encapsulated enzyme was investigated and compared to encapsulated enzyme within polypyrrole. The data presented herein show that at the same experimental conditions the glucose oxidase, if encapsulated within polypyrrole, is more stable than native enzyme. (C) 2012 Elsevier B.V. All rights reserved.