Molecular chaperone-like properties of sodium caseinate to suppress the pressure-induced aggregation of -lactoglobulin
Molecular chaperone-like properties of sodium caseinate to suppress the pressure-induced aggregation of -lactoglobulin
复制标题
酪蛋白酸钠的分子伴侣特性可抑制压力诱导的乳球蛋白聚集
DOI：
10.1080/08957959.2019.1575967
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发表时间：
2019
影响因子：
2
通讯作者：
Azuma Norihiro
中科院分区：
文献类型：
--
作者：
He Jin Song;Gao Qing;Mu Tai Hua;Azuma Norihiro
本研究的目的是确定酪蛋白酸钠是否可以抑制压力处理诱导的乳清蛋白聚集。将β-乳球蛋白（β-Lg，0.2%，w/v）的溶液以及含有0.2%（w/v）β-Lg和0-0.5%（w/v）酪蛋白酸钠（NaCas）的混合物在400-800 MPa下加压。 NaCas能抑制压力诱导的β-Lg聚集，且这种作用具有浓度依赖性。此外，NaCas通过抑制β-Lg聚集体从可溶相向不溶性相的转变，改变了β-Lg的聚集过程，从而降低了不溶性聚集体的比例。在此过程中，NaCas与变性的β-Lg形成稳定的复合物，复合物的形成阻止了β-Lg的进一步聚集。
The objective of this study was to determine whether sodium caseinate can inhibit the aggregation of whey protein induced by pressure treatment. Solutions of β-lactoglobulin (β-Lg, 0.2%, w/v) and mixtures containing 0.2% (w/v) β-Lg and 0–0.5% (w/v) sodium caseinate (NaCas) were pressurized at 400–800 MPa. NaCas suppressed the aggregation of β-Lg induced by pressure treatment, and this function was dependent on the concentration of NaCas. Furthermore, NaCas altered the aggregation process of β-Lg by suppressing the transition of the aggregate from the soluble phase to the insoluble phase and, as a result, the fraction of insoluble aggregates was decreased. During this process, NaCas formed stable complexes with the denatured β-Lg, and the formation of complexes prevented further aggregation of β-Lg. These results indicate that NaCas exhibits a chaperone-like activity under high pressure.