Non-covalent immobilization of quince (Cydonia oblonga) polyphenol oxidase on alumina
Küçük Resim Yok
Tarih
2002
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Slovensko Kemijsko Drustvo
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
Polyphenol oxidase enzyme purified partially from quince (Cydonia oblonga) was immobilized on alumina (Al2O3) by simple adsorption at pH 6.8. The properties of immobilized enzyme were compared to those of the free enzyme. Optimum pH (8.5) and temperature (45 degreesC) were determined, showing the alteration of pH and temperature profiles by immobilization. Catechol, L-DOPA, p-cresole and pyrogallol were tested as substrate and it was established that affinity was highest for catechol. K-m constant was 5 mM for catechol. Thermal and storage stability were carried out. It was observed that the immobilized enzyme had storage stability for a period of one year.
Açıklama
Anahtar Kelimeler
Alumina, Polyphenol Oxidase, Purification, Non-Covalent, Immbolization, Tyrosinase, Phenols, Purification, Electrodes, Water
Kaynak
Acta Chimica Slovenica
WoS Q Değeri
Q3
Scopus Q Değeri
Q3
Cilt
49
Sayı
4
