A comparison of Polyphenoloxidases from different plants

Arabacı, Gülnur

dc.contributor.authors	Arabaci, G; Duzcan, B;
dc.date.accessioned	2020-02-24T14:14:20Z
dc.date.available	2020-02-24T14:14:20Z
dc.date.issued	2009
dc.identifier.citation	Arabaci, G; Duzcan, B; (2009). A comparison of Polyphenoloxidases from different plants. FEBS JOURNAL, 276, 128-128
dc.identifier.issn	1742-464X
dc.identifier.uri	https://hdl.handle.net/20.500.12619/44724
dc.identifier.uri	https://doi.org/10.1080/10942910903453363
dc.description.abstract	Artichoke polyphenol oxidases (PPOs) were obtained by (NH4)2SO4 precipitation using ascorbic acid, polyvinylpyrrolidone, and Triton X-100. The PPO content of artichoke head (AHPPO) was 8820 units (mg protein)−1 as compared with 3370 units (mg protein)−1 in artichoke leaves-and-stem (ALSPPO) by using catechol as a substrate. The substrates of both AHPPO and ALSPPO are o-diphenols, such as catechol, pyrogallol, and L-DOPA. Optimum pH and temperature of both PPOs were determined. AHPPO had higher thermal stability than ALSPPO. Also, Tm (the midpoint of thermal inactivation) and t1/2 (half-life) values were determined. Km and Vmax of both PPOs were observed to be similar. Twelve inhibitors were tested and their I50 values were determined. The most effective inhibitors were found to be potassium cyanide, ascorbic acid, L-cysteine, and thiourea. Sodiumdodecylsulfate, urea, and cupric sulfate caused an increase about 20–30% in the PPO activity.
dc.language	English
dc.publisher	WILEY-BLACKWELL PUBLISHING, INC
dc.subject	Biochemistry & Molecular Biology
dc.title	A comparison of Polyphenoloxidases from different plants
dc.type	Meeting Abstract
dc.identifier.volume	276
dc.identifier.startpage	128
dc.identifier.endpage	128
dc.contributor.department	Sakarya Üniversitesi/Fen-Edebiyat Fakültesi/Kimya Bölümü
dc.contributor.saüauthor	Arabacı, Gülnur
dc.relation.journal	FEBS JOURNAL
dc.identifier.wos	WOS:000267069900353
dc.contributor.author	Arabacı, Gülnur