数字农科院2.0

Mild acid extraction of Camellia protein with low saponin: Composition identification and interfacial stabilization

文献类型： 外文期刊

作者： Yang, Xiaoli;Zhou, Jisong;Fu, Qingxuan;Jin, Weiping;Shen, Wangyang;Tian, Yaoqi;Peng, Dengfeng

作者机构：

关键词： Camellia proteins;Foamability;Emulsifying property;Composition;Mild acid extraction;Proteomic

期刊名称： FOOD HYDROCOLLOIDS

ISSN： 0268-005X

年卷期： 2024 年 160 卷

页码：

收录情况： SCIE（2024版） ; ; EI（2024版）

摘要： The long-standing challenge of Camellia protein use is eliminating the saponins in the extraction process, as a high level of saponins imparts an off-taste. Here, we designed a mild acid (pH 6.0) and high-salt (0.5-3.0 M) extraction using NaCl, KCl, CaCl2, and MgCl2 solutions as solvents, which realized a protein yield of 71.2-81.4%. After dialysis, almost 90% of the saponins in the Camellia protein was removed. Through proteomic analysis, the proteins in Camellia albumin were shown to include Bet v I/major latex protein domain-containing protein, adenylate kinase, and acyl-CoA-binding protein, which are related to cellular components and endogenous enzymes. The identified Camellia globulin was a cupin type-1 domain-containing protein, belonging to the 11S globulin storage proteins. Both Camellia albumin and globulin competent stabilized air-water and oil-water interfaces. Notably, the foamability and emulsifying activity index of albumin at a concentration of 1 mg/mL reached 300% and 176 m2/g, respectively. This study demonstrated a convenient and efficient means to extract Camellia albumin and globulin with low levels of saponins, clarified the composition and structure of the extracted proteins, and illustrated their potential application as highly effective interfacial stabilizers in the food, cosmetic, and pharmaceutical industries.

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