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中国精品科技期刊2020
李政奇,孙卓妍,张秀清,等. 盐溶法制备菜籽蛋白的工艺优化及其理化特性研究J. 食品工业科技,2026,47(15):280−288. doi: 10.13386/j.issn1002-0306.2025070313.
引用本文: 李政奇,孙卓妍,张秀清,等. 盐溶法制备菜籽蛋白的工艺优化及其理化特性研究J. 食品工业科技,2026,47(15):280−288. doi: 10.13386/j.issn1002-0306.2025070313.
LI Zhengqi, SUN Zhuoyan, ZHANG Xiuqing, et al. Optimization of Rapeseed Protein Preparation by Salt Extraction and Its Physiochemical PropertiesJ. Science and Technology of Food Industry, 2026, 47(15): 280−288. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2025070313.
Citation: LI Zhengqi, SUN Zhuoyan, ZHANG Xiuqing, et al. Optimization of Rapeseed Protein Preparation by Salt Extraction and Its Physiochemical PropertiesJ. Science and Technology of Food Industry, 2026, 47(15): 280−288. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2025070313.

盐溶法制备菜籽蛋白的工艺优化及其理化特性研究

Optimization of Rapeseed Protein Preparation by Salt Extraction and Its Physiochemical Properties

  • 摘要: 本文以冷榨脱皮菜籽饼为原料,采用单因素及响应面试验系统优化了盐溶法制备菜籽蛋白的工艺,并与碱溶酸沉法菜籽蛋白的物化特性进行比较研究。结果表明,在对原料进行植酸酶-含水乙醇预处理的基础上,盐溶法制备菜籽蛋白的最佳工艺参数为:0.75 mol/L离子强度的CaCl2提取介质、pH6.5、料液比1:12 g/mL、53 ℃条件下浸提90 min,该条件下蛋白溶出率为27.96%;经透析后得到的菜籽蛋白与碱溶酸沉法菜籽蛋白相比,具有较高的蛋白纯度(77.12%±0.63%)及较低的植酸含量(0.13%±0.01%);此外,SDS-PAGE结果显示盐溶法菜籽蛋白富含白蛋白,二级结构中以α-螺旋和β-转角为主,结构兼具稳定性和灵活性,同时具有较优的溶解性能。本实验为盐溶法制备高品质菜籽蛋白提供了基础。

     

    Abstract: The aim of the study was to provide a reference basis for the preparation of high-quality rapeseed protein by salt-extraction. Cold-pressed dehulled rapeseed meal was used. The salt-extraction process was optimized using single-factor experiment and response surface experiments analysis, and the physicochemical properties were investigated and compared with the protein obtained by alkali-extraction and acid-precipitation. The results showed that the optimal conditions were as follows, pretreatment with phytase and hydrated ethanol, 0.75 mol/L CaCl2 extracting medium, pH6.5, solid-liquid ratio 1:12 g/mL, temperature 53 ℃ and extraction time 90 minutes, and achieving a protein solubility of 27.96% under these conditions. Furthermore, the resulted rapeseed protein achieved a higher protein purity at 77.12%±0.63% and a lower phytic acid content of 0.13%±0.01%, in comparison to the protein obtained by alkali-extraction and acid-precipitation method. What's more, SDS-PAGE analysis revealed that the main components of salt-extracted protein were albumin. Its higher contents of α-helices and β-turns dominated its stable and flexible structure, also leading to better solubility. This experiment provides a basis for using the salt-solution method to prepare high-quality rapeseed protein.

     

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