Improved chromatographic method for purification of lactoperoxidase from different milk sources
Yazarlar (4)
Zeynep Köksal İstanbul Medeniyet Üniversitesi, Türkiye
Dr. Öğr. Üyesi Hande USANMAZ Sinop Üniversitesi, Türkiye
Songül Bayrak
Prof. Dr. Hasan Özdemir Atatürk Üniversitesi, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY (Q4) | ||
| Dergi ISSN | 1082-6068 Dergi Bilgileri (2017) | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | İngilizce | Basım Tarihi | 01-2017 |
| Kabul Tarihi | – | Yayınlanma Tarihi | 03-11-2016 |
| Cilt / Sayı / Sayfa | 47 / 2 / 129–136 | DOI | 10.1080/10826068.2016.1185732 |
| Makale Linki | http://dx.doi.org/10.1080/10826068.2016.1185732 | ||
| UAK Araştırma Alanları |
Biyokimya
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| Özet |
| Our previous studies showed that sulfanilamide is a new competitive inhibitor of and can be used in the purification of lactoperoxidase (LPO, EC1.11.1.7) from milk. However, this method has some disadvantages like a lower purification factor. The aim of the present study is to improve the purification process of milk LPO from different sources. For this purpose, 16 commercial sulfanilamide derivatives were selected for inhibition studies to determine the best inhibitor of bovine LPO by calculating kinetic parameters. A cyanogen bromide-activated Sepharose 4B affinity matrix was synthesized by coupling with each competitive inhibitor. Among the inhibitors, 5-amino-2-methylbenzenesulfonamide and 2-chloro-4-sulfamoylaniline were used as ligands for the purification of LPO from bovine, buffalo, cow, and goat milks with 1059.37, 509.09, 232.55, and 161.90, and 453.12-, 151.86-, 869.00-, and 447.57-fold … |
| Anahtar Kelimeler |
| Affinity chromatography | enzyme purification | lactoperoxidase | mammalian milk |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| Web of Science | 19 |
| Google Scholar | 24 |