Non-covalent immobilization of quince (Cydonia oblonga) polyphenol oxidase
Küçük Resim Yok
Tarih
2002
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Tubitak Scientific & Technological Research Council Turkey
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
A partially purified polyphenol oxidase from quince (Cydonia oblonga) was immobilized on bentonite by simple adsorption at pH 6.8. The properties of the immobilized enzyme were compared to those of the free enzyme. Optimum pH and temperature were determined to be 9.0 and 45degreesC, respectively, showing the alteration of pH and temperature profiles by immobilization. No drastic change was observed in the K-m value after immobilization. Catechol, L-DOPA, p-cresole and pyrogallol were tested as substrates. Thermal and storage stability and reusability experiments were carried out. It was observed that the immobilized enzyme had storage stability for a period of one year but had no reusability in the batch process.
Açıklama
Anahtar Kelimeler
Bentonite, Polyphenol Oxidase, Purification, Non-Covalent Immobilization, Characterization, Tyrosinase, Purification, Phenols, Electrodes, Water
Kaynak
Turkish Journal Of Chemistry
WoS Q Değeri
Q3
Scopus Q Değeri
Q3
Cilt
26
Sayı
5
