Yagar, HulyaKocaturk, Selin2024-06-122024-06-1220142169-14012169-141Xhttps://doi.org/10.3109/21691401.2013.808648https://hdl.handle.net/20.500.14551/18268Polyphenol 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.en10.3109/21691401.2013.808648info:eu-repo/semantics/openAccessAlginateArtichokeCarrageenanCatecholase ActivityCresolase ActivityEntrapmentPolyphenol OxidaseCynara-Scolymus L.L-Dopa ProductionImmobilized TyrosinaseNylon 6,6PurificationStabilityHeadsBeadsArticle424268273Q4WOS:0003398025000072-s2.0-8490435899023795723Q1