Kemoterapötik Bir Ajan Olan L-asparaginazın Farklı Polimerik Yapılara İmmobilizasyonu ve Karakterizasyonu
2014
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Advisor: Doç. Dr. Burhan Ateş
Abstract (EN)
L-asparaginase, is the enzyme effectively used to treatment of acute lymphoblastic leukemia (ALL). Polyethylene glycol (PEG) conjugation of the enzyme is quite common to solve the hypersensitive reaction which is limit in the use of L-asparaginase. However, a different biocompatible material by immobilization of L-asparaginase is very important to use more effectively. The purpose of this study has prepared at different biocompatible polymeric structures to be used for immobilization of L-asparaginase and the immobilized enzyme is tested of availability as both structural and kinetically. In our study, different rates starch blended polymethylmethacrylate (PMMA), polyhydroxyethylmethacrylate (PHEMA) and polymethacrylic acid : polymethylmethacrylate P(MA-MMA) polymeric structures were prepared as the solid matrix. All structures were characterized with FTIR, TGA, DTA, DSC and liquid contact angle, structurally. With starch added to the polymeric structure was found to increase the biodegradability of the polymeric structure, lower the liquid contact angle and extend the decomposition temperature range. In the immobilization of L-asparaginase, 3% for PHEMA and PMMA, 5% for P(MMA-MA) starch-containing polymer exhibited the highest activity values. Immobilized enzymes were found to retain activity compare with free enzyme at the temperatures above of 50 °C. Especially, P(MA-MMA)-5N-Asn samples was determined at the half-life of immobilized enzyme to be prolonged up to 30 days at room temperature. As a result, biocompatible polymeric structures have been revealed for more effective use and immobilization of L-asparaginase.
Author
Dr. Ahmet Ulu
How to Cite
Ahmet Ulu (Master Thesis). Kemoterapötik Bir Ajan Olan L-asparaginazın Farklı Polimerik Yapılara İmmobilizasyonu ve Karakterizasyonu, 2014, İnönü University.
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