Lizine duyarlı enzim elektrodunu geliştirilmesi
İmproving enzyme electrode for l-lysine
- Tez No: 58298
- Danışmanlar: DOÇ. DR. GÜLEREN ÖZKAN
- Tez Türü: Yüksek Lisans
- Konular: Kimya, Chemistry
- Anahtar Kelimeler: L-Lysine, L-lysine decarboxylase, Amino asitler, Lizin, L-Lysine, L-lysine decarboxylase, Amino acids, Lysine
- Yıl: 1997
- Dil: Türkçe
- Üniversite: Ankara Üniversitesi
- Enstitü: Fen Bilimleri Enstitüsü
- Ana Bilim Dalı: Kimya Ana Bilim Dalı
- Bilim Dalı: Belirtilmemiş.
- Sayfa Sayısı: Belirtilmemiş.
Özet
ABSTRACT Masters Thesis IMPROVING ENZYME ELECTRODE FOR L-LYSINE Nilüfer VURAL (CANLI ) Ankara Unxversity Graduate School of Natural and Applied Sciences Department of Chemistry Supervisor: Assoc. Prof. Dr.Güleren ÖZKAN 1997, Page: 104 Jury : Prof. Dr. Ali Osman SOLAK Assoc. Prof. Dr. Kamuran AYHAN Assoc. Prof. Dr. Güleren ÖZKAN L-Lysine is one of essential amino acid and economically important biotechnological products. It is the first limiting amino acid in cereals and therefore finds wire application as supplement in animal feed. A simple and sensitive technique with bacterial L-Lysine decarboxylase for the determination of L-Lysine is reported. This method involves a decarboxylation of L-Lysine to produce carbon dioxide and the potentiometric determination of this product with carbon dioxide gas-sensing electrode. In this study E. coll was cultured under aerobic conditions and lysine decarboxylase was purified to homogenity from E. coll. The enzyme exhibited Michaelis-Menten kinetics toward L-Lysine. Using this method the Kb, for Lysine decarboxylase from E. coll is found as 2.0 mM. The value obtained showed good agreement with that reported in literature. The experiment demonstrate that Lysine decarboxylase can be applied in a rapid and reliable determination of L-Lysine. The optimum pH was 6.0, and the optimum temperature was 37 °C. The purified lysine decarboxylase is active only when freshly prepared.
Özet (Çeviri)
ABSTRACT Masters Thesis IMPROVING ENZYME ELECTRODE FOR L-LYSINE Nilüfer VURAL (CANLI ) Ankara Unxversity Graduate School of Natural and Applied Sciences Department of Chemistry Supervisor: Assoc. Prof. Dr.Güleren ÖZKAN 1997, Page: 104 Jury : Prof. Dr. Ali Osman SOLAK Assoc. Prof. Dr. Kamuran AYHAN Assoc. Prof. Dr. Güleren ÖZKAN L-Lysine is one of essential amino acid and economically important biotechnological products. It is the first limiting amino acid in cereals and therefore finds wire application as supplement in animal feed. A simple and sensitive technique with bacterial L-Lysine decarboxylase for the determination of L-Lysine is reported. This method involves a decarboxylation of L-Lysine to produce carbon dioxide and the potentiometric determination of this product with carbon dioxide gas-sensing electrode. In this study E. coll was cultured under aerobic conditions and lysine decarboxylase was purified to homogenity from E. coll. The enzyme exhibited Michaelis-Menten kinetics toward L-Lysine. Using this method the Kb, for Lysine decarboxylase from E. coll is found as 2.0 mM. The value obtained showed good agreement with that reported in literature. The experiment demonstrate that Lysine decarboxylase can be applied in a rapid and reliable determination of L-Lysine. The optimum pH was 6.0, and the optimum temperature was 37 °C. The purified lysine decarboxylase is active only when freshly prepared.
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