乳铁蛋白
变性(裂变材料)
乳清蛋白
乳清蛋白
化学
动力学
色谱法
作文(语言)
β-乳球蛋白
分离乳清蛋白粉
α-乳清蛋白
生物化学
食品科学
核化学
哲学
物理
量子力学
语言学
作者
Amira Halabi,Amélie Deglaire,Pascaline Hamon,Saı̈d Bouhallab,Didier Dupont,Thomas Croguennec
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2019-07-29
卷期号:302: 125296-125296
被引量:52
标识
DOI:10.1016/j.foodchem.2019.125296
摘要
The process of manufacturing infant milk formulas (IMFs) involves heat treatments that can lead to whey protein denaturation. The objective of the study was to determine how protein composition affects the denaturation kinetics of the whey proteins within IMFs. Three model IMFs (1.3% of cow's milk protein) were produced with a caseins: whey proteins ratio of 40:60, differing only by the whey protein composition. The kinetics of heat-induced denaturation of α-lactalbumin, β-lactoglobulin and lactoferrin were investigated between 67.5 °C and 80 °C by chromatographic quantification of the residual native proteins. Results showed that the heat-denaturation of α-lactalbumin was reduced when β-lactoglobulin was absent. The heat-denaturation of lactoferrin was not affected by the composition of the IMFs but its presence enhanced the heat-denaturation of β-lactoglobulin. This study revealed that, for higher heat treatments (90 °C/15 s, 75 °C/15 min), IMF containing α-lactalbumin and lactoferrin preserved a higher proportion of native whey proteins than IMFs containing β-lactoglobulin.
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