目的:分析苦荞麸皮粉中蛋白含量及其蛋白组成。方法:采用碱法提取-等电点沉淀分离蛋白。在单因素试验基础上,选取料液比(w/v)、pH、时间等3个影响因素,采用响应面法(Box-Behnken中心组合)优化苦荞麸皮粉蛋白提取工艺。结果:料液比、pH...目的:分析苦荞麸皮粉中蛋白含量及其蛋白组成。方法:采用碱法提取-等电点沉淀分离蛋白。在单因素试验基础上,选取料液比(w/v)、pH、时间等3个影响因素,采用响应面法(Box-Behnken中心组合)优化苦荞麸皮粉蛋白提取工艺。结果:料液比、pH、时间对麸皮蛋白提率有显著影响,影响顺序为料液比>pH>时间。响应面优化得到最佳提取条件为pH 10.5、料液比1∶35、时间3 h 40 min,此条件下苦荞麸皮蛋白提取率为(97.31±4.64)%。结论:本研究为有效开发利用苦荞麸皮粉的蛋白提供科学依据。展开更多
Fourier transform infrared spectroscopy(FTIR) and circular dichroism(CD) were used to investigate the conformational changes of heated whey protein(WP) and the corresponding changes in the hydrolysates immunoreactivit...Fourier transform infrared spectroscopy(FTIR) and circular dichroism(CD) were used to investigate the conformational changes of heated whey protein(WP) and the corresponding changes in the hydrolysates immunoreactivity were determined by competitive enzyme-linked immunosorbent assay(ELISA).Results showed that the contents of α-helix and β-sheet of WP did not decrease much under mild heating conditions and the antigenicity was relatively high;when the heating intensity increased(70 ℃ for 25 min or 75 ℃ for 20 min),the content of α-helix and β-sheet decreased to the minimum,so was the antigenicity;However,when the WP was heated at even higher temperature and for a longer time,the β-sheet associated with protein aggregation begun to increase and the antigenicity increased correspondingly.It was concluded that the conformations of heated WP and the antigenicity of its hydrolysates are related and the optimum structure for decreasing the hydrolysates antigeniity is the least content of α-helix and β-sheet.Establishing the relationship between the WP secondary structure and WP hydrolysates antigenicity is significant to supply the reference for antigenicity reduction by enzymolysis.展开更多
文摘目的:分析苦荞麸皮粉中蛋白含量及其蛋白组成。方法:采用碱法提取-等电点沉淀分离蛋白。在单因素试验基础上,选取料液比(w/v)、pH、时间等3个影响因素,采用响应面法(Box-Behnken中心组合)优化苦荞麸皮粉蛋白提取工艺。结果:料液比、pH、时间对麸皮蛋白提率有显著影响,影响顺序为料液比>pH>时间。响应面优化得到最佳提取条件为pH 10.5、料液比1∶35、时间3 h 40 min,此条件下苦荞麸皮蛋白提取率为(97.31±4.64)%。结论:本研究为有效开发利用苦荞麸皮粉的蛋白提供科学依据。
基金National Science and Technology Support Program(2009BADB9B06)Beijing Science and Technology Program(D10110504601002)
文摘Fourier transform infrared spectroscopy(FTIR) and circular dichroism(CD) were used to investigate the conformational changes of heated whey protein(WP) and the corresponding changes in the hydrolysates immunoreactivity were determined by competitive enzyme-linked immunosorbent assay(ELISA).Results showed that the contents of α-helix and β-sheet of WP did not decrease much under mild heating conditions and the antigenicity was relatively high;when the heating intensity increased(70 ℃ for 25 min or 75 ℃ for 20 min),the content of α-helix and β-sheet decreased to the minimum,so was the antigenicity;However,when the WP was heated at even higher temperature and for a longer time,the β-sheet associated with protein aggregation begun to increase and the antigenicity increased correspondingly.It was concluded that the conformations of heated WP and the antigenicity of its hydrolysates are related and the optimum structure for decreasing the hydrolysates antigeniity is the least content of α-helix and β-sheet.Establishing the relationship between the WP secondary structure and WP hydrolysates antigenicity is significant to supply the reference for antigenicity reduction by enzymolysis.