As a valuable tree nut, walnut is a well-known member of the Juglandaceae family. The fruit is made up of an outer green shell cover or husk, the middle shell which must be cracked to release the kernel, a thin layer known as skin or the seed coat, and finally, the kernel or meat. The nutritional importance of walnut fruit is ascribed to its kernel. The shell and husk are burned as fuel or discarded away as waste products. In the past two decades, the evaluation of the phenolic content and antioxidant activity of different parts of walnut has received great interest. In this contribution, the recent reports on the extraction and quantification of phenolic content from each part of the walnut tree and fruit using different solvents were highlighted and comparatively reviewed. The current review paper also tries to describe the antioxidant content of phenolic extracts obtained from different parts of the walnut tree and fruit. Additionally, the antioxidant and antiradical activities of the prepared extracts have also been discussed.

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The walnut (Juglans spp.) is an appreciated nut that belongs to the Juglandaceae family. The fruit includes four main parts: the kernel, the skin, the shell, and the green husk. It is widely cultivated due to its edible kernel. In walnut production centers, high amounts of the husk as an agro-forest waste product are produced and discarded away. Recently, it has been demonstrated that the walnut green husk could be valued as a source of different natural bioactive compounds with excellent antioxidant and antimicrobial properties. Regarding this respect, in this contribution, the current scientific knowledge on the antioxidant and antiradical activities, various identified and isolated individual chemical constituents, as well as the functional applications of the walnut husk with more emphasis on the Persian walnut (Juglans regia L.) are reviewed.

The objective of present study was in vitro and in vivo evaluation of hepatoprotective and antioxidant activity of Quercetin nanoparticles (Q NPs) against toxicity induced by aflatoxin B1. The Q NPs were prepared using precipitation method. Hepatocytes were prepared by the method of collagenase enzyme perfusion via portal vein. The NPs were characterized in terms of size and morphology using dynamic light scattering (DLS) and transmission electron microscopy (TEM), respectively. The level of parameters, such as cell death, ROS formation, lipid peroxidation, mitochondrial membrane potential and cellular glutathione (GSH) content, in the aflatoxin B1-treated and non-treated hepatocytes were determined and the mentioned markers were assessed in the presence of Q NPs. The prepared NPs showed particle size of 52.70 nm with polydispersity index (PDI) of 0.18. In contrast to free Q, the administration of Q NPs more efficiently decreased the rate of ROS formation, lipid peroxidation and improved cell viability, mitochondrial membrane potential and glutathione level and showed a significant hepatoprotective efiect by reducing levels of aspartate aminotransferase, alanine aminotransferase and alkaline phosphatase. It is suggested that the Q NPs is a promising candidate for drug delivery, which enhances the hepatoprotective effect of Q against the cytotoxic effects of aflatoxin B1.

Thymol is the main monoterpene phenol present in the essential oils which is used in the food industry as flavoring and preservative agent. In this study, the interaction of thymol with the concentration range of 1 to 6 μM and bovine serum albumin (BSA) at fixed concentration of 1 μM was investigated by fluorescence, UV-vis, and molecular docking methods under physiological-like condition. Fluorescence experiments were performed at 5 different temperatures, and the results showed that the fluorescence quenching of BSA by thymol was because of a static quenching mechanism. The obtained binding parameters, K, were in the order of 10 M , and the binding number, n, was approximately equal to unity indicating that there is 1 binding site for thymol on BSA. Calculated thermodynamic parameters for enthalpy (ΔH), entropy (ΔS), and Gibb's free energy (ΔG) showed that the reaction was spontaneous and hydrophobic interactions were the main forces in the binding of thymol to BSA. The results of UV-vis spectroscopy and Arrhenius' theory showed the complex formation in the interaction of thymol and BSA. Negligible conformational changes in BSA by thymol were observed in fluorescence experiments, and the same results were also obtained from UV-vis studies. Results of molecular docking indicated that the subdomain IA of BSA was the binding site for thymol.