Comparison of some biochemical properties of artichoke polyphenol oxidase entrapped in alginate-carrageenan and alginate gels
dc.contributor.author | Yagar, Hulya | |
dc.contributor.author | Kocaturk, Selin | |
dc.date.accessioned | 2024-06-12T10:51:10Z | |
dc.date.available | 2024-06-12T10:51:10Z | |
dc.date.issued | 2014 | |
dc.department | Trakya Üniversitesi | en_US |
dc.description.abstract | 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. | en_US |
dc.description.sponsorship | Research Fund of Trakya University [TUBAP-821] | en_US |
dc.description.sponsorship | This research was funded by Research Fund of Trakya University (TUBAP-821). | en_US |
dc.identifier.doi | 10.3109/21691401.2013.808648 | |
dc.identifier.endpage | 273 | en_US |
dc.identifier.issn | 2169-1401 | |
dc.identifier.issn | 2169-141X | |
dc.identifier.issue | 4 | en_US |
dc.identifier.pmid | 23795723 | en_US |
dc.identifier.scopus | 2-s2.0-84904358990 | en_US |
dc.identifier.scopusquality | Q1 | en_US |
dc.identifier.startpage | 268 | en_US |
dc.identifier.uri | https://doi.org/10.3109/21691401.2013.808648 | |
dc.identifier.uri | https://hdl.handle.net/20.500.14551/18268 | |
dc.identifier.volume | 42 | en_US |
dc.identifier.wos | WOS:000339802500007 | en_US |
dc.identifier.wosquality | Q4 | en_US |
dc.indekslendigikaynak | Web of Science | en_US |
dc.indekslendigikaynak | Scopus | en_US |
dc.indekslendigikaynak | PubMed | en_US |
dc.language.iso | en | en_US |
dc.publisher | Informa Healthcare | en_US |
dc.relation.ispartof | Artificial Cells Nanomedicine And Biotechnology | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/openAccess | en_US |
dc.subject | Alginate | en_US |
dc.subject | Artichoke | en_US |
dc.subject | Carrageenan | en_US |
dc.subject | Catecholase Activity | en_US |
dc.subject | Cresolase Activity | en_US |
dc.subject | Entrapment | en_US |
dc.subject | Polyphenol Oxidase | en_US |
dc.subject | Cynara-Scolymus L. | en_US |
dc.subject | L-Dopa Production | en_US |
dc.subject | Immobilized Tyrosinase | en_US |
dc.subject | Nylon 6,6 | en_US |
dc.subject | Purification | en_US |
dc.subject | Stability | en_US |
dc.subject | Heads | en_US |
dc.subject | Beads | en_US |
dc.title | Comparison of some biochemical properties of artichoke polyphenol oxidase entrapped in alginate-carrageenan and alginate gels | en_US |
dc.type | Article | en_US |