State Key Laboratory of Food Science and Resources, Nanchang University, Nanchang 330047, China.
College of Food Science and Technology, Nanchang University, Nanchang 330031, China.
J Agric Food Chem. 2024 Aug 14;72(32):17771-17781. doi: 10.1021/acs.jafc.4c04827. Epub 2024 Aug 1.
As the demand for lactoferrin increases, the search for cost-effective alternative proteins becomes increasingly important. Attention naturally turns to other members of the transferrin family such as ovotransferrin. The iron-binding abilities of these proteins influence their characteristics, although the underlying mechanisms remain unclear. This overview systematically summarizes the effects of the iron-binding ability on the fate of food-derived transferrins (lactoferrin and ovotransferrin) and their potential applications. The findings indicate that iron-binding ability significantly influences the structure of food-derived transferrins, particularly their tertiary structure. Changes in structure influence their physicochemical properties, which, in turn, lead to different behaviors in response to environmental variations. Thus, these proteins exhibit distinct digestive characteristics by the time they reach the small intestine, ultimately performing varied physiological functions . Consequently, food-derived transferrins with different iron-binding states may find diverse applications. Understanding this capability is essential for developing food-derived transferrins and driving innovation in lactoferrin-related industries.
随着乳铁蛋白需求的增加，寻找具有成本效益的替代蛋白质变得越来越重要。人们自然会关注转铁蛋白家族的其他成员，如卵转铁蛋白。这些蛋白质的铁结合能力影响其特性，尽管其潜在机制尚不清楚。本文系统地总结了铁结合能力对食物来源转铁蛋白（乳铁蛋白和卵转铁蛋白）命运的影响及其潜在应用。研究结果表明，铁结合能力显著影响食物来源转铁蛋白的结构，特别是其三级结构。结构的变化会影响其理化性质，进而导致其对环境变化的不同反应。因此，这些蛋白质在到达小肠时表现出不同的消化特性，最终发挥不同的生理功能。因此，具有不同铁结合状态的食物来源转铁蛋白可能会有不同的应用。了解这种能力对于开发食物来源转铁蛋白和推动乳铁蛋白相关产业的创新至关重要。
