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| 大豆肽钙螯合物的制备、稳定性及表征 |
| Preparation, stability and characterization of calcium-binding peptides from soybean meal |
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| DOI： |
| 中文关键词: 大豆肽钙螯合物 制备 稳定性 表征 |
| 英文关键词:calcium-binding peptides from soybean meal preparation stability characterization |
| 基金项目:国家自然科学基金（31201380） |
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| 中文摘要: |
| 豆粕通过醇洗、酸沉、水解工艺制备大豆肽，并将大豆肽与钙离子进行螯合反应，制备大豆肽钙螯合物。测定了大豆肽钙螯合物的氨基酸组成及在磷酸盐溶液中、不同pH下的稳定性，并对大豆肽钙螯合物进行DSC、TGA、Zeta电位、XRD分析。结果表明：大豆肽钙螯合物的钙结合量为5303 mg/g，与CaCl2相比，大豆肽钙螯合物具有更高的钙保留率；具有较高钙螯合能力的大豆肽的相对分子质量主要集中在小于1 kDa的范围内；大豆肽与钙离子螯合后，谷氨酸和天冬氨酸含量由34.33%提高至49.83%；大豆肽钙螯合物在不同pH条件下均未发生较大程度的解离；大豆肽与钙离子反应后，电负值由-37.73 mV降到-12.32 mV；大豆肽钙螯合物在XRD图谱中的衍射峰收窄，峰值由20°偏移至22.5°，同时在42.5°出现1个微弱的衍射峰，且氯化钙的特征峰消失，表明大豆肽与钙离子形成了新的化合物；大豆肽钙螯合物具有更好的热稳定性。 |
| 英文摘要: |
| Soybean peptides were prepared from defatted soybean meal by alcohol washing, acid precipitation and hydrolysis process. Then the soybean peptides were chelated with calcium ions to prepare calcium-binding peptides from soybean meal.The amino acid composition and stabilities of the calcium-binding peptides from soybean meal in the phosphate solution and at different pH were determined, and the DSC, TGA, Zeta potential and XRD of calcium-binding peptides from soybean meal were analyzed, The results showed that the calcium-binding amount of calcium-binding peptides from soybean meal was 53.03 mg/g,and the calcium-binding peptides from soybean meal had a higher calcium retention rate than CaCl2. The relative molecular weight of soybean peptides with higher calcium chelating ability mainly concentrated in the range of less than 1 kDa. The contents of glutamic acid and aspartic acid increased from 34.33% to 49.83% after the reaction of soybean peptides with calcium ions. The calcium-binding peptides from soybean meal did not dissociate in a large extent under various pH conditions. The Zeta potential value of soybean peptides decreased from -37.73 mV to -12.32 mV after reaction with calcium ions. The diffraction peak of the calcium-binding peptides from soybean meal in the XRD pattern was narrowed, the peak shifted from 20° to 22.5°, and a weak diffraction peak appeared at 425°, and the characteristic peak of calcium chloride disappeared, which indicated that the reaction of soybean peptides and calcium ions formed new compounds. The calcium-binding peptides from soybean meal had better thermal stability. |
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