Physicochemical and functional properties of a protein isolate from maca (Lepidium meyenii) and the secondary structure and immunomodulatory activity of its major protein component
Physicochemical and functional properties of a protein isolate from maca (Lepidium meyenii) and the secondary structure and immunomodulatory activity of its major protein component
复制标题
玛咖（Lepidium meyenii）分离蛋白的理化和功能特性及其主要蛋白成分的二级结构和免疫调节活性
DOI：
10.1039/c8fo02490a
复制
发表时间：
2019
期刊：
影响因子：
6.1
通讯作者：
Wu Hui
中科院分区：
文献类型：
--
作者：
Wu Liying;Zhang Mengmeng;Xin Xuan;Lai Furao;Wu Hui
从猕猴桃根中提取了猕猴桃分离蛋白(MPI)，并对其理化和功能性质以及主要蛋白质组分基质金属蛋白酶的二级结构和免疫调节活性进行了研究。与大豆分离蛋白(SPI)和酪蛋白相比，MPI缺乏必需氨基酸，但富含半胱氨酸和脯氨酸。其表面疏水性(H0,812.4)、吸油量(7.4g−1)、起泡性(100%)和乳化活性(58.2g−1)均高于大豆分离蛋白。但MPI的热稳定性(Td，87.4℃)、起泡稳定性(75%)和乳化稳定性(26.3min)均弱于SPI。MMP五聚体的相对分子质量为22 kDa，富含β-Sheet。基质金属蛋白酶能显著增强RAW 264.7细胞的吞噬能力，促进NO、肿瘤坏死因子α和IL 6的分泌，主要涉及Toll样受体4和补体受体3。
Maca protein isolate (MPI) was extracted from maca root, and its physicochemical and functional properties, and the secondary structure and immunomodulatory activity of its major protein component, MMP, were investigated. The MPI lacked essential amino acids compared with soybean protein isolate (SPI) and casein, but was rich in cysteine and proline. The MPI had rich free sulfhydryl (20.6 μmol g−1), and its surface hydrophobicity (H0, 812.4), oil absorption capacity (7.4 g g−1), foaming capacity (100%) and emulsifying activity (58.2 m2 g−1) were higher than that of SPI. However, the thermal stability (Td, 87.4 °C), foaming stability (75%) and emulsifying stability (26.3 min) of the MPI were weaker than that of the SPI. MMP was a pentamer with a molecular weight of 22 kDa and rich in β-sheets. MMP could significantly enhance the phagocytic capacity and promote the NO, TNF-α and IL-6 secretion of RAW 264.7 cells, involving toll-like receptor 4 and complement receptor 3 mainly.