Preparation and properties of ?-galactosidase chemically attached to activated chitin
Küçük Resim Yok
Tarih
2003
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
?-Galactosidase (?-D-galactoside galactohydrolase, EC 3.2.1.22) from watermelon was covalently immobilized on chitin. The immobilized ?-galactosidase exhibited an activity of 0.61 U per g of carrier and an activity yield of 67%. The properties of free and immobilized ?-galactosidase were also searched and compared. The results showed that, optimum conditions for activity were not affected by immobilization. The optimum pH and temperature for free and immobilized enzyme found as pH 6.0 and 65°C, respectively. Compared with the free enzyme, the temperature and pH stabilities of the immobilized enzyme were similar. Both the enzymes were stable between pH 2-10 and below 50°C. The Km values for free and immobilized enzyme were determined using p-nitrophenyl-?-D-galactopyranoside (PNPG) and raffinose as substrates. Operational stability of the immobilized enzyme was investigated by using both substrates. The operational half-life (t 1/2) was calculated as 34 h for PNPG and 28 h for raffinose. The immobilized ?-galactosidase was also utilized in the hydrolysis of raffinose. The immobilization procedure on chitin was cheap and also easy to carry out, and the immobilized enzyme had good properties that the potential for practical application is considerable.
Açıklama
Anahtar Kelimeler
?-Galactosidase, 1,1'-Carbonyldiimidazole, Chitin, Covalent attachment, Immobilization, Raffinose, Watermelon
Kaynak
Artificial Cells, Blood Substitutes, and Immobilization Biotechnology
WoS Q Değeri
Scopus Q Değeri
N/A
Cilt
31
Sayı
3
