Which casein in sodium caseinate is most resistant to in vitro digestion? Effect of emulsification and enzymatic structuring
Which casein in sodium caseinate is most resistant to in vitro digestion? Effect of emulsification and enzymatic structuring
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DOI：
10.1016/j.foodhyd.2018.09.042
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发表时间：
2019-03-01
影响因子：
10.7
通讯作者：
Macierzanka, Adam
中科院分区：
文献类型：
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作者：
Bottger, Franziska;Dupont, Didier;Macierzanka, Adam
我们研究了食品级乳蛋白酪蛋白酸钠（NaCN）中单个组分酪蛋白表位（α S-1-、α S-2-、β-和kappa-CN）对模拟人胃十二指肠消化的抗性。采用间接ELISA法研究了NaCN在油包水乳状液液滴表面的吸附以及蛋白质与转谷氨酰胺酶（TG）交联对蛋白质水解的影响。TG交联使得酪蛋白分子片段显著地抵抗消化。然而，这取决于酪蛋白的类型以及NaCN是否以溶液或乳液形式存在。发现交联显著阻碍NaCN的主要酪蛋白之一β-CN中的几个氨基酸区域的消化。对于α S-1-和α S-2-CN，在NaCN在溶液中交联而不是在乳液中交联（或在有限程度上交联）后，仅观察到对消化酶的有限抗性。kappa-CN被证明是最不耐酶水解，无论TG处理。我们的工作首次展示了重要食品级蛋白质成分的单个组分的消化率在复杂的胶体食品系统中如何不同。它还显示了如何通过化学和物理结构调节消化率的例子。
We investigated the resistance of individual constituent casein epitopes (alpha S-1-, alpha S-2-, beta- and kappa-CN) in food-grade milk protein sodium caseinate (NaCN) to simulated human gastro-duodenal digestion. The influence of NaCN adsorption to the surface of oil-in-water emulsion droplets and the effect of crosslinking of the protein with enzyme transglutaminase (TG) on the proteolysis were studied by indirect ELISA. TG crosslinking rendered fragments of casein molecules significantly resistant to digestion. However, it depended on the type of casein and whether NaCN was presented in solution or emulsion. The crosslinking was found to considerably hinder the digestion of several amino acid regions in one of the major caseins of NaCN, beta-CN. For alpha S-1- and alpha S-2-CN, only limited resistance to digestive enzymes was observed after NaCN had been crosslinked in solution but not (or to a limited extent) in emulsion. kappa-CN proved to be the least resistant to the enzymatic hydrolysis regardless of the TG treatment. Our work shows for the first time how the digestibility of individual components of important food-grade protein ingredients can differ in a complex, colloidal food system. It also shows an example of how the digestibility can be modulated by chemical and physical structuring.