Sunflower seeds contain a high amount of chlorogenic acid (3-4% in weight) and a specific polyphenoloxidase that oxidize it. In this research, the activity of a sunflower seed enzymatic solution was investigated in vivo and in vitro on endogenous and exogenous chlorogenic acid. Phenol degradation was monitored by spectrophotometric analysis at 325 and 420 nm or by HPLC analysis. It was ascertained that during the germination, sunflower seeds synthesized an enzyme like-polyphenoloxidase after 24 h that got dark the seedlings ground and degraded endogenous chlorogenic acid. Sunflower-seedling like-polyphenoloxidase enzyme could be easily isolated in active form. Enzymatic extract catalysed in vitro the degradation of chlorogenic and also caffeic acid. In comparison to original value, after 60 min of incubation under environment temperature and pH 7, chlorogenic and caffeic acid have been reduced by 64 and the 90%, respectively. A high linear correlation was verified between enzymatic activity and original concentration of chlorogenic acid in a range from 0.01 to 0.1 mM. This linear correlation suggested a possible use of like-polyphenoloxidase enzyme for analytical application and other biotechnological uses in the treatment of medium containing natural phenols.
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