Effect and mechanism of freezing on the quality and structure of soymilk gel induced by different salt ions

文献类型： 外文期刊

第一作者： Xia, Xiaoyu

作者： Xia, Xiaoyu;Yang, Xinxin;Zhu, Ying;Sun, Ying;Zhu, Xiuqing;Xia, Xiaoyu;Zhu, Xiuqing

作者机构：

关键词： soymilk gel; salt ion; freezing; gelation rate; texture; protein structure

期刊名称：JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE （ 影响因子：4.1； 五年影响因子：4.2 ）

ISSN： 0022-5142

年卷期： 2024 年

页码：

收录情况： SCI

摘要： BACKGROUNDThe increasing attention toward frozen soy-based foods has sparked interest. Variations exist in the quality and structure of soymilk gels induced by different salt ions, leading to diverse changes post-freezing. This study compared and analyzed the effects of calcium chloride (CC), magnesium chloride (MC) and calcium sulfate (CS) on the quality characteristics and protein structure changes of soymilk gels (CC-S, MC-S and CS-S) before and after freezing, and clarified the mechanisms of freezing on soymilk gel.RESULTSThe formation rate of soymilk gel is influenced by the type of salt ions. In comparison to CS and MC, soymilk gel induced by CC exhibited the fastest formation rate, highest gel hardness, lowest moisture content, and smaller gel pores. However, freezing treatment deteriorated the quality of soymilk gel induced by different salt ions, leading to a decline in textural properties (hardness and chewiness). Among these, the textual state of CC-induced soymilk gel remained optimal, exhibiting the least apparent damage and minimal cooking loss. Freezing treatments prompt a transition of soymilk gel secondary structure from beta-turns to beta-sheets, disrupting the protein's tertiary structure. Furthermore, freezing treatments also fostered the crosslinking between soymilk gel protein, increasing the content of disulfide bonds.CONCLUSIONThe quality of frozen soymilk gel is influenced by the rate of gel formation induced by salt ions. After freezing, soymilk gel with faster gelation rates exhibited a greater tendency for the transformation of protein-water interactions into protein-protein interactions. They showed a higher degree of disulfide bond formation, resulting in a more tightly knit and firm frozen gel network structure with denser and more uniformly distributed pores. (c) 2024 Society of Chemical Industry.

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