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Cynarin is a derivative of hydroxycinnamic acid and it has biologically active functional groups constituent of some plants and food. We elucidated the antioxidant activity of cynarin by using different in vitro condition bioanalytical antioxidant assays like DMPD : 0.9444) and 39.34 ± 13.88 nM, respectively. This study clearly showed that cynarin had marked antioxidant, anticholinergic, reducing ability, radical-scavenging, and metal-binding activities.

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In this study, the influence of milled crust and flour from oleaster (Elaeagnus angustifolia L.) separately added at different levels (1%, 2% and 3%) on the physical, chemical, sensory, colour properties and antioxidant properties of ice creams were investigated. The increment of crust and flour level caused an increase of dry matter, acidity, viscosity, first dripping, complete melting and vitamin C content. Flour increased overrun values in ice cream. Our results indicated that lyophilised oleaster extracts contain remarkable phenolic compounds. It was observed that lyophilised oleaster extracts exhibited a moderate in vitro antioxidant capacity. The addition of oleaster flour and crust positively affected sensory properties. The sensory results showed that ice cream containing 2% oleaster flour was the highest scored by the panellists. Oleaster flour and crust increased the sweetness of ice cream samples. These results showed that considerable nutritive and functional improvement could be attained by the addition of oleaster flour to ice cream formulation so that it could be used as natural antioxidants in ice cream as a source of flavour with complacency.

Lignans are a large group of chemical compounds found in plants. They have effects on enzymes, protein synthesis, cell proliferation, angiogenesis, growth factor and cell differentiation. In this study, inhibition effects of α-(-)-conidendrin, enterodiole, enterolactone, nordihydroguaiaretic acid, secoisolariciresinol and secoisolariciresinol diglucoside against carbonic anhydrase I and II isoenzymes (CA I, and II) and acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes were investigated. The Ki values of the lignans were found to be in the ranges of 1.27-3.30 nM for CA I, 1.11-2.68 nM for CA II, 0.72-1.62 nM for AChE, and 0.08-0.20 nM for AChE.