Improved chromatographic method for purification of lactoperoxidase from different milk sources

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dc.authoridgerni, serpil/0000-0001-7699-1697
dc.authoridBAYRAK, SONGUL/0000-0001-6424-2760
dc.authoridUSANMAZ, HANDE/0000-0003-3851-9601
dc.contributor.authorKoksal, Zeynep
dc.contributor.authorUsanmaz, Hande
dc.contributor.authorBayrak, Songul
dc.contributor.authorOzdemir, Hasan
dc.date.accessioned2025-03-23T19:34:55Z
dc.date.available2025-03-23T19:34:55Z
dc.date.issued2017
dc.departmentSinop Üniversitesi
dc.description.abstractOur 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, respectively. Our results show that 5-amino-2-methylbenzenesulfonamide, 2-chloro-4sulfamoylaniline, and 5-amino-1-naphthalenesulfonamide are the best inhibitors for one-step purification of the enzyme.
dc.description.sponsorshipTUBITAK [114Z038]; TUBITAK
dc.description.sponsorshipThis study was supported by TUBITAK (Project number: 114Z038). We are thankful to TUBITAK for their support.
dc.identifier.doi10.1080/10826068.2016.1185732
dc.identifier.endpage136
dc.identifier.issn1082-6068
dc.identifier.issn1532-2297
dc.identifier.issue2
dc.identifier.pmid27191680
dc.identifier.scopus2-s2.0-84994168594
dc.identifier.scopusqualityQ2
dc.identifier.startpage129
dc.identifier.urihttps://doi.org/10.1080/10826068.2016.1185732
dc.identifier.urihttps://hdl.handle.net/11486/5766
dc.identifier.volume47
dc.identifier.wosWOS:000394995600004
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTaylor & Francis Inc
dc.relation.ispartofPreparative Biochemistry & Biotechnology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WOS_20250323
dc.subjectAffinity chromatography
dc.subjectenzyme purification
dc.subjectlactoperoxidase
dc.subjectmammalian milk
dc.titleImproved chromatographic method for purification of lactoperoxidase from different milk sources
dc.typeArticle

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