Phenol oxidase activity of a monogenean, Paramazocraes thrissocles

1986 ◽  
Vol 60 (3) ◽  
pp. 234-238
Author(s):  
T. Thangaraj ◽  
A. Vinayakam ◽  
K. Nellaiappan

AbstractThe phenol oxidase of a monogenean, Paramazocraes thrissocles, oxidizes phenolic amines more effectively than other phenols studied. Based on the substrate specificity, the probable substrate for eggshell formation has been suggested. The enzyme shows the pH optimum of 7–2. At 40°C it shows maximum activity. Proenzyme is activated by metal ions and detergents. Copper chelating compounds strongly inhibit the enzyme.

Wetlands ◽  
2018 ◽  
Vol 39 (2) ◽  
pp. 263-273 ◽  
Author(s):  
Kevan J. Minick ◽  
Alexia M. Kelley ◽  
Guofang Miao ◽  
Xuefeng Li ◽  
Asko Noormets ◽  
...  

2017 ◽  
Vol 105 ◽  
pp. 108-110 ◽  
Author(s):  
Magdalena M. Wiedermann ◽  
Evan S. Kane ◽  
Timothy J. Veverica ◽  
Erik A. Lilleskov

1986 ◽  
Vol 60 (3) ◽  
pp. 201-209 ◽  
Author(s):  
A. Bhagavathiammai ◽  
K. Ramalingam

AbstractCytochemical localization of the enzyme phenol oxidase inNeomurraytrema tengrahas been studied. Results reveal that the enzyme reacts with substrates such as catechol, hydroquinone, pyrogallol, dopa, doparmine, epinephrine and tyramine, but not with tyrosine and protocatechuic acid. Thus it shows activity with a wide range of phenols, aminated, mono and diphenols and also with deaminated and decarboxylated, di- and polyphenols. The maximum activity of the enzyme occurs between 40°C and 50°C with a pH optimum of 6–6.


2007 ◽  
Vol 71 (3) ◽  
pp. 319-324 ◽  
Author(s):  
Carine Floch ◽  
Enrique Alarcon-Gutiérrez ◽  
Stéven Criquet

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