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dc.contributor.authorErgün, Adem
dc.contributor.authorArslan, Oktay
dc.date.accessioned2019-10-08T11:39:48Z
dc.date.available2019-10-08T11:39:48Z
dc.date.issued2016en_US
dc.identifier.issn1742-464X
dc.identifier.uri1742-4658
dc.identifier.urihttps://hdl.handle.net/20.500.12462/6756
dc.description.abstractPolyphenol oxidase (PPO) enzyme, sometimes called as phenoloxidase, catecholase, phenolase, catechol oxidase or tyrosinase, isconsidered to be an o-dipenol. PPO (EC 1.14.18.1), a multifunc-tional copper containing metalloenzyme, is widely distributed innature. PPO exists in many kinds of plants and fungi, such asbanana, mushroom, butter lettuce, Napoleon grape, potato, cof-fee, marula fruit, artichoke heads, longan fruit, tobacco, wheatflour.In this study, a novel affinity chromatography gel was synthe-sized for purifing PPO enzyme. The affinity chromatography gelwas synthesized by coupling aniline as a specer arm to CNBractiveted Sepharose-4B. Then, p-amino benzoic acid was coupledto aniline as a ligand. PPO was purified fromMusa sapientum var. Cavendishii(banana) by using Sepharose-4B-aniline p-aminobenzoic acid affinity chromatography gel. % 4.49 yield and 33.4fold purification were achieved. SDS-polyacrylamide gel elec-trophoresis of the enzyme indicates a single band with an appar-ent MW of 35 kDa. The Vmaxand Kmof the purified enzymewere determined 42,628 U/ml min and 9.27 mM, respectively.en_US
dc.language.isoengen_US
dc.publisherWiley-Blackwellen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.titleA new affinity gel for purifing polyphenol oxidase enzymeen_US
dc.typeotheren_US
dc.relation.journalFebs Journalen_US
dc.contributor.departmentFen Edebiyat Fakültesien_US
dc.identifier.volume283en_US
dc.identifier.startpage333en_US
dc.identifier.endpage333en_US
dc.relation.publicationcategoryDiğeren_US


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