Influence of Ternary Complexation between Bovine Serum Albumin, Sodium Phytate, and Divalent Salts on Turbidity and In Vitro Digestibility of Protein,Journal of Agricultural and Food Chemistry

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Influence of Ternary Complexation between Bovine Serum Albumin, Sodium Phytate, and Divalent Salts on Turbidity and In Vitro Digestibility of Protein
Journal of Agricultural and Food Chemistry ( IF 5.7 ) Pub Date : 2018-09-18 00:00:00 , DOI: 10.1021/acs.jafc.8b03142
Elaine Kaspchak ₁ , Luciana Igarashi-Mafra ₁ , Marcos R. Mafra ₁

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Phytate decreases mineral and protein availability and influences protein properties, such as solubility and stability. The binding constants and turbidity data can help with the understanding of the influence of phytate and divalent salts on protein behavior. Ternary complexes formed between bovine serum albumin, sodium phytate, and divalent salts were investigated by isothermal titration calorimetry, turbidity, and in vitro protein digestibility. Results showed a positive entropy change and a negative and small enthalpy change as a result of electrostatic binding forces and ternary and binary complex precipitation. The interaction was favored for the systems containing calcium and manganese, whereas those containing magnesium showed a low heat of interaction. Despite the high protein digestibility, the stability of divalent phytates in a wide pH range may decrease mineral bioavailability. These results can provide important insights for the study of mineral bioavailability and diverse processes that involve protein and minerals in several areas of knowledge.

中文翻译：

牛血清白蛋白，植酸钠和二价盐三元络合对蛋白质浊度和体外消化率的影响

植酸降低了矿物质和蛋白质的利用率，并影响蛋白质的性质，例如溶解性和稳定性。结合常数和浊度数据可以帮助理解肌醇六磷酸和二价盐对蛋白质行为的影响。通过等温滴定热法，浊度和体外研究了牛血清白蛋白，植酸钠和二价盐之间形成的三元复合物蛋白质消化率。结果表明，由于静电结合力以及三元和二元复合物的沉淀，熵的正变化为负，焓的变化为负。对于含钙和锰的体系，该相互作用是有利的，而含镁的体系显示出较低的相互作用热。尽管蛋白质具有很高的消化率，但二价植酸在宽pH范围内的稳定性可能会降低矿物质的生物利用度。这些结果可为研究矿物质的生物利用度和涉及蛋白质和矿物质的多种知识的多种过程提供重要的见识。

更新日期：2018-09-18

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