scholarly journals Purification and Some Properties of Chlorogenic Acid Oxidase from Apple(Malus pumila)

1992 ◽  
Vol 56 (11) ◽  
pp. 1705-1710 ◽  
Author(s):  
Masatsune Murata ◽  
Chiyo Kurokami ◽  
Seiichi Homma
Author(s):  
S. J. Sheen

AbstractThe percent incorporation of chlorogenic acid, chlorogenic acid oxidase (CAO), peroxidase (PRO) and Fraction I protein into the non-dialyzable fraction of acid-precipitated and acid-soluble brown pigments of tobacco was studied by use of


1987 ◽  
Vol 51 (10) ◽  
pp. 2843-2844
Author(s):  
Tetsuzo Tono ◽  
Shuji Fujita ◽  
Hirotaka Kawasaki ◽  
Zhong-Fu Li

1987 ◽  
Vol 51 (10) ◽  
pp. 2843-2844 ◽  
Author(s):  
Tetsuzo TONO ◽  
Shuji FUJITA ◽  
Hirotaka KAWASAKI ◽  
Zhong-Fu LI

2006 ◽  
Vol 32 (6) ◽  
pp. 275-281 ◽  
Author(s):  
Yunzhe HAN ◽  
Ayumu MAMIYA ◽  
Eline NKYA ◽  
Nobuyuki HAYASHI ◽  
Shuji FUJITA

1986 ◽  
Vol 41 (1-2) ◽  
pp. 56-60 ◽  
Author(s):  
Jeremy M. Boniwell ◽  
Vernon S. Butt

Abstract Particulate preparations from potato tubers, extracted in 4 mᴍ 2-m ercaptoethanol, catalyze the 3-hydroxylation of 4-hydroxyphenylpropanoid carboxylic acids, including p-coumaric acid and tyrosine, in the presence of NADH (or NADPH) and FAD (or FMN); ascorbate could not substitute for these electron donors. Among a range of 4-hydroxylated C6-C2 and C6-C1 compounds tested, only 4-hydroxyphenylacetic acid and p-cresol were hydroxylated. The hydroxylase was sensitive to KCN and diethyldithiocarbam ate and showed some features of phenolase hydroxylation, but no DOPA oxidase nor chlorogenic acid oxidase activity was exhibited under these conditions. It is suggested that the phenolase complex, which is confined to potato tuber particles, in whole or part catalyzes the hydroxylation.


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