Affinity purification and characterization of polyphenol oxidase from helianthus tuberosus L.

Erzengin, Mahmut

Affinity purification and characterization of polyphenol oxidase from helianthus tuberosus L.

dc.contributor.author	Erzengin, Mahmut
dc.date.accessioned	2019-05-30T11:31:17Z
dc.date.available	2019-05-30T11:31:17Z
dc.date.issued	2009
dc.department	Sabire Yazıcı Fen Edebiyat Fakültesi
dc.description.abstract	Polyphenol oxidase (PPO) of Jerusalem artichoke (Helianthus Tuberosus L.) tubers was purified using a Sepharose-4B-L-tyrosine-p-amino benzoic acid affinity gel. Both nativeand SDS-gel electrophoresis analyses of the purified PPO gave a single band (ca. 65 kDa based on SDS-PAGE), indicating that it is a monomer. The purified PPO showed activity towards diphenolic and triphenolic substrates but not with the monophenolic substrates, suggesting that it lacks monophenolase activity. The optimum temperature and pH values vary between 20-35oC and 5.0-8.0, respectively, depending on the substrate used; for catechol, the optimum temperature and pH values were found to be 20oC and 7.0, respectively. The purified enzyme was relatively stable at 40oC but unstable at higher temperatures. Furthermore, IC50 values for various inhibitors and inhibition modes were also determined using catechol as a substrate; ?-mercaptoethanol showed the strongest inhibition, followed by 2-mercapto benzothiazol, glutathione, L-cysteine and dithioerythritol, respectively
dc.identifier.endpage	325	en_US
dc.identifier.issn	1303-5002
dc.identifier.issue	4	en_US
dc.identifier.startpage	313	en_US
dc.identifier.uri	https://hdl.handle.net/20.500.12451/1137
dc.identifier.volume	37	en_US
dc.indekslendigikaynak	TR-Dizin
dc.language.iso	en
dc.publisher	Hacettepe Üniversitesi
dc.relation.ispartof	Hacettepe Journal of Biology and Chemistry
dc.relation.publicationcategory	Makale - Ulusal Hakemli Dergi - Kurum Öğretim Elemanı
dc.rights	info:eu-repo/semantics/openAccess
dc.subject	Jerusalem artichoke (Helianhtus tuberosus L.)
dc.subject	Polyphenol Oxidase
dc.subject	Affinity Chromatography
dc.subject	Substrate Specificity
dc.subject	Activation Energy
dc.subject	Heat Inactivation
dc.subject	Inhibition
dc.subject	Helianthus Tuberosus
dc.subject	Yerelması
dc.subject	Katekol Oksidaz
dc.subject	Kromatografi
dc.subject	Yem Bitkileri
dc.subject	Isı
dc.subject	Engelleme
dc.subject	Fenolik Bileşikler
dc.subject	Saflaştırma
dc.subject	Substrat
dc.subject	Aktivasyon Enerjisi
dc.subject	Polifenol Oksidaz
dc.title	Affinity purification and characterization of polyphenol oxidase from helianthus tuberosus L.
dc.type	Article