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Hen egg albumen is commonly used for in vitro anti-inflammatory assay by thermal protein denaturation. There are many sources of albumen such as from eggs of quail, pigeon, hen, duck, goose, and crocodile. Thus, this study aims to investigate alternative sources of albumen that can be used for this assay. Albumen specimens collected from quail, pigeon, hen, duck, goose, and crocodile eggs were employed for investigating protein denaturation by turbid formation after 5 min incubation at 70ºC and 85ºC, following standard protocol. The amount of protein of each albumen was determined spectrophotometrically at 280 nm using bovine serum albumin as standard protein. Then, albumen exhibiting a turbidity response similar to that of hen egg albumen was selected to determine anti-inflammatory activity using diclofenac sodium as a positive control. Our results show that only quail egg albumen became turbid after being heated at 70oC for 5 min in a way similar to hen albumen, with absorbance values of 1.341 ± 0.006 and 1.134 ± 0.016 Absorbance units (AU), respectively. The other egg albumen specimens showed low turbidity values of between 0.013-0.175 AU. After increasing the incubation temperature to 85oC, the turbidity of quail, duck, and goose egg albumen specimens was increased. The least amount of protein was evident for crocodile egg albumen (5.64 ± 0.39 mg/0.2 ml of albumen), while the other sources contained 26.4-31.7 mg/0.2 ml of albumen. There was no relation found between the turbidity and amount of protein except for crocodile egg albumen. The IC50 values for hen and quail egg albumens were 1092 and 625 µg/ml, respectively. This indicated that quail egg albumen exhibited higher sensitivity for thermal protein denaturation than hen egg albumen. We propose that quail egg albumen, which is inexpensive and available in some countries, may be used instead of hen egg albumen for in vitro anti-inflammatory activity assay using the thermal protein denaturation inhibition technique.
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