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Serum albumins such as bovine (BSA) and human (HSA) serum albumins are abundant serum proteins, which act as transport carrier in blood plasma with abundance 52-60%. Because of having multiple lipophilic binding sites located in subdomains IIA and IIIA, serum albumins are capable of transporting and distributing of endogenous and exogenous compounds like various ligands, vitamins, hormones, drugs, nutrients, food additives and other physiological substances. With increasing the amount of binding affinity between these proteins and compounds, free concentration and the physiological activity of various materials such as drugs decreased in blood plasma. Therefore, the investigation of binding affinity between serum albumins and various compounds are essential. In addition, BSA is large monomeric protein (66kDa) with a single chain of 583 amino acid residues and isoelectric point around 4.7–5.2 that share around 76% structural homology with HSA.
Food additives have been widely used in food industry in order to preserve flavor of foods or improve its taste and appearance in recent decades. Propyl gallate (PG) is an example of phenolic antioxidant agents that added to unsaturated vegetable oils, fats and meat products for prevention from oxidation process.