Chemical Engineering Department, Federal University of Paraná, Polytechnic Center, Jardim das Américas, 81531-980 Curitiba, PR, Brazil.
Chemical Engineering Department, Federal University of Paraná, Polytechnic Center, Jardim das Américas, 81531-980 Curitiba, PR, Brazil.
Food Chem. 2018 Jun 30;252:1-8. doi: 10.1016/j.foodchem.2018.01.089. Epub 2018 Jan 12.
Bioavailability of food nutrients can be reduced in the presence of antinutrients such as phytates and tannins. This work aimed to study bovine serum albumin binding to phytic acid and tannic acid, and its influence on in vitro protein digestibility. The effect of autoclaving and boiling on protein digestibility and the microstructure of complexes was also evaluated. Results showed that high ionic strength promotes greater affinity between tannic acid and bovine serum albumin, and decreases in vitro protein digestibility. For phytic acid and bovine serum albumin, the opposite behavior is observed because interactions are governed by electrostatic forces. A rise in temperature above that causing denaturation of the protein favors its interaction with phytic acid, and disfavors that with tannic acid, probably due to different protein binding site exposure. For both antinutrients, heating treatment increased protein hydrolysis, the size of complexes and their fragility.
抗营养因子如植酸和单宁酸的存在会降低食物营养素的生物利用度。本研究旨在研究牛血清白蛋白与植酸和单宁酸的结合及其对体外蛋白质消化率的影响。还评估了高压灭菌和煮沸对蛋白质消化率和复合物微观结构的影响。结果表明，高离子强度促进单宁酸与牛血清白蛋白之间更大的亲和力，并降低体外蛋白质消化率。对于植酸和牛血清白蛋白，观察到相反的行为，因为相互作用受静电力控制。温度升高超过导致蛋白质变性的温度有利于其与植酸相互作用，而不利于与单宁酸相互作用，这可能是由于不同的蛋白质结合位点暴露所致。对于这两种抗营养因子，热处理均增加了蛋白质水解、复合物的大小及其脆性。
