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中国精品科技期刊2020
栾慧琳,华晓晗,于文华,等. 基于制备工艺变化探究大豆蛋白钙结合能力与结构相关性[J]. 食品工业科技,2025,46(2):47−56. doi: 10.13386/j.issn1002-0306.2023120282.
引用本文: 栾慧琳,华晓晗,于文华,等. 基于制备工艺变化探究大豆蛋白钙结合能力与结构相关性[J]. 食品工业科技,2025,46(2):47−56. doi: 10.13386/j.issn1002-0306.2023120282.
LUAN Huilin, HUA Xiaohan, YU Wenhua, et al. Relationship Between Calcium-binding Ability and Structure of Soybean Protein Based on the Change of Preparation[J]. Science and Technology of Food Industry, 2025, 46(2): 47−56. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023120282.
Citation: LUAN Huilin, HUA Xiaohan, YU Wenhua, et al. Relationship Between Calcium-binding Ability and Structure of Soybean Protein Based on the Change of Preparation[J]. Science and Technology of Food Industry, 2025, 46(2): 47−56. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023120282.

基于制备工艺变化探究大豆蛋白钙结合能力与结构相关性

Relationship Between Calcium-binding Ability and Structure of Soybean Protein Based on the Change of Preparation

  • 摘要: 大豆蛋白是优质的植物基替代蛋白,但相比动物蛋白仍存在钙含量较低的缺陷。本研究测定了不同碱溶酸沉提取工艺、热处理与酶解处理条件下大豆蛋白的钙结合能力,并比较了四种不同制备方式下,大豆蛋白的钙结合能力、亚基组成、二级结构、三级结构以及疏水性的差别,讨论了大豆蛋白钙结合能力与结构的关系。结果表明,大豆蛋白与钙离子的结合与大豆蛋白的二级结构组成和疏水性密切相关。热处理与酶解处理都会使大豆蛋白二级结构展开,疏水性增强,暴露出更多的钙结合位点。但酶解后小分子量蛋白的疏水性聚集,使蛋白空间结构发生改变,对大豆蛋白钙结合能力的改善要优于热处理的效果,结合态钙含量提高了53%。热-酶复合处理大豆蛋白(Heat-enzyme complex treatment of soybean protein,H-SPHs)效果最佳,结合物得率与结合态钙占比均提高了2倍,沉淀率降低了43%,此时大豆蛋白的制备工艺条件为:碱溶pH8、碱溶温度25 ℃、酸沉蛋白与水质量比1:4、中和pH8、100 ℃热处理30 min、1000 U/g风味蛋白酶酶解3 h。

     

    Abstract: Soybean protein was a high-quality plant-based alternative protein, yet its calcium content was lower than animal protein. This study measured the calcium-binding ability of soybean protein under different extraction, heat treatment, and enzymatic hydrolysis conditions. The differences in calcium-binding ability, subunit composition, secondary structure, tertiary structure and hydrophobicity of soybean protein under four different preparation methods were compared. The relationship between the calcium-binding ability and the structure of soybean protein were discussed. The results showed that the binding of soybean protein and calcium ions was related to both the protein's secondary structure composition and its hydrophobicity. Heat treatment and enzymatic hydrolysis unfolded the secondary structure, leading to the enhancement of hydrophobicity and the exposure of the calcium-binding sites. Enzymolysis led to the aggregation of small molecular weight proteins, causing a spatial restructuring of the protein. These changes resulted in a 53% increase in bound calcium compared to heat treatment. The heat-enzyme combined treatment was the most effective among various treatments, which could increase the Ca2+ of the protein by about 2 folds and decrease the precipitation rate by 43%. Optimal soybean protein with high calcium-binding ability preparation involved dissolution at pH8 and 25 ℃, with acid-precipitated proteins dissolved in four times water at pH8. Subsequent steps included heating at 100 ℃ for 30 minutes, and enzymatic treatment using 1000 U/g flavor protease for three hours.

     

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