Document Type : Original Articles
Authors
1
Department of Primatology, IPB University, Bogor, Indonesia
2
School of Veterinary Medicine and Biomedical Sciences, IPB University, Bogor, Indonesia
3
Primate Research Center, IPB University, Bogor, Indonesia
4
Veterinary Study Program, Padjadjaran University, Sumedang, Indonesia
5
Department Research and Development, PT. Biomol Nusantara Mandiri, Bandung, Indonesia
6
Biotechnology Study Program, Padjadjaran University, Bandung, Indonesia
7
Veterinary Study Program, Faculty of Medicine, Sumedang, Indonesia
10.22092/ari.2026.371600.4013
Abstract
Immunoglobulin Y (IgY) is a promising alternative antibody with broad applications in immunotherapy, diagnostics, and passive immunization due to its low production cost, non-invasive extraction, and high yield from egg yolk. In addition, IgY offers several biological advantages over mammalian IgG, including the absence of interaction with mammalian Fc receptors and the inability to activate the human complement system, making it safer for biomedical and veterinary applications. However, the functional stability of IgY can be compromised by environmental stressors such as elevated temperature, extreme pH conditions, and exposure to digestive enzymes, which may limit its effectiveness in various formulations and delivery routes. This study aimed to evaluate IgY stability using the Agar Gel Precipitation Test (AGPT), a simple and low-cost qualitative method capable of detecting antigen–antibody interactions through visible precipitin line formation. Purified IgY was exposed to different temperatures (room temperature to 70°C), pH conditions (3–9), and digestive enzymes (pepsin at pH 3 and trypsin at pH 8) for 15, 30, and 60 minutes prior to AGPT evaluation. The intensity and clarity of precipitin lines were used as indicators of preserved antigen-binding activity. The results demonstrated that IgY maintained strong precipitin intensity at temperatures up to 60°C, under neutral to alkaline pH conditions, and following exposure to trypsin. In contrast, exposure to 70°C and pepsin at pH 3 resulted in markedly reduced precipitin intensity. Physical coagulation of IgY was also observed at 70°C, indicating heat-induced denaturation and loss of functional integrity. Overall, this study demonstrates that AGPT is an effective and practical preliminary screening tool for assessing IgY stability under various physicochemical and enzymatic stress conditions, particularly in laboratories with limited access to advanced analytical techniques, before further quantitative or structural analyses are conducted.
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