Comparison of some biochemical properties of artichoke polyphenol oxidase entrapped in alginate-carrageenan and alginate gels
Küçük Resim Yok
Tarih
2014
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Informa Healthcare
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Polyphenol oxidase (PPO, EC.1.14.18.1) isolated from artichoke (Cynara scolymus) was entrapped within alginate and alginate+ carrageenan beads, and the catecholase and cresolase activities of both entrapped enzymes were determined. Some properties of these immobilized enzymes such as optimum pH and temperature, kinetic parameters (K-m and V-max), thermal, and storage stability were determined and compared to each other. The highest catecholase activity was observed in alginate gel (370 U/g bead) while the highest cresolase activity was in alginate+ carrageenan gel (90 U/g bead). For catecholase and cresolase activities, optimum pHs of alginate and alginate+ carrageenan beads were determined to be 7.0 and 4.0, respectively. Optimum temperatures for catecholase activity were determined to be 40 degrees C for both entrapped enzymes. These values for cresolase activity were 30 degrees C and 20 degrees C, respectively. Immobilized artichoke PPOs greatly preserved their thermal stability which exists anyway. The catalytic efficiency value (V-max/K-m) of the alginate beads is approximately high as two-and-a-half folds of that of alginate+kappa-carrageenan beads for cresolase activity. These values were very close for catecholase activity. Immobilized beads saved their both activities after 30 days of storage at 4 degrees C.
Açıklama
Anahtar Kelimeler
Alginate, Artichoke, Carrageenan, Catecholase Activity, Cresolase Activity, Entrapment, Polyphenol Oxidase, Cynara-Scolymus L., L-Dopa Production, Immobilized Tyrosinase, Nylon 6,6, Purification, Stability, Heads, Beads
Kaynak
Artificial Cells Nanomedicine And Biotechnology
WoS Q Değeri
Q4
Scopus Q Değeri
Q1
Cilt
42
Sayı
4
