花生球蛋白、伴花生球蛋白及亚基含量显著影响蛋白质的凝胶性和溶解性等功能特性,进而影响其在肉制品、植物蛋白饮料中的应用效果。目前常采用提取蛋白质后再用电泳及光密度法测定球蛋白、伴球蛋白及亚基含量的方法,操作步骤繁琐,样品...花生球蛋白、伴花生球蛋白及亚基含量显著影响蛋白质的凝胶性和溶解性等功能特性,进而影响其在肉制品、植物蛋白饮料中的应用效果。目前常采用提取蛋白质后再用电泳及光密度法测定球蛋白、伴球蛋白及亚基含量的方法,操作步骤繁琐,样品损失量大。为此收集了178个花生品种,分别提取蛋白,采用电泳法测定球蛋白、伴球蛋白、23.5和37.5 kDa亚基含量并获得大量数据的基础上,利用近红外光谱技术进行整粒花生样品的光谱扫描,将其与传统方法测定的化学值进行拟合,采用偏最小二乘回归(PLSR)化学计量法构建数学模型。通过比较单一和复合光谱预处理方式,对比模型相关系数和误差评估预测模型性能。确定球蛋白模型最佳预处理方法为2^(nd)-der with Detrend,校正集相关系数为0.92,标准差为1.41;伴球蛋白模型最佳预处理方法为Detrend with 1^(st)-der,校正集相关系数为0.85,标准差为1.46;23.5 kDa亚基含量模型最佳预处理方法为Normalization with 2^(nd)-der,校正集相关系数为0.91,标准差为0.53;37.5 kDa模型最佳预处理方法为Detrend with Baseline,校正集相关系数为0.91,标准差为0.89。外部验证结果表明,球蛋白预测均方根误差(square errors of predi ction,SEP)为1.25,伴球蛋白SEP为0.73,23.5 kDa模型SEP为0.47,37.5 kDa模型SEP为0.75。本研究基于近红外光谱技术实现了对整粒花生进行球蛋白、伴球蛋白、23.5 kDa和37.5 kDa亚基含量的同步、快速和无损检测,为育种专家加工专用品种选育和蛋白加工企业原料选用提供了根据。展开更多
本文通过Zeta电位、内源荧光光谱、粒度、SDS-PAGE凝胶电泳及溶解性,探讨花生球蛋白和伴花生球蛋白在酸性条件下亚基结构的变化规律。电泳分析表明,花生球蛋白40.5、37.5、35.5和27 ku亚基在常温p H 2.0-3.0的条件下被酸解,产生32.86...本文通过Zeta电位、内源荧光光谱、粒度、SDS-PAGE凝胶电泳及溶解性,探讨花生球蛋白和伴花生球蛋白在酸性条件下亚基结构的变化规律。电泳分析表明,花生球蛋白40.5、37.5、35.5和27 ku亚基在常温p H 2.0-3.0的条件下被酸解,产生32.86±0.10ku的新亚基,同时22和15 ku这两条亚基增多;当p H〈2.0时,花生球蛋白的亚基酸解受静电屏蔽抑制。当p H为1.0-3.0,伴花生球蛋白Ⅱ61 ku亚基被酸解产生36.95±0.50、25.14±1.86、18.98±0.78和17.37±1.17 ku这四个条带。进一步研究表明,花生球蛋白和伴花生球蛋白在酸性条件下结构伸展,粒径增大,在p H 2.0-3.0时的Zeta电位及溶解度较高。在p H 2.0-3.0内,花生球蛋白荧光扫描最大发射波长相对中性条件下发生红移,红移幅度大于伴球蛋白,说明伴球蛋白展开程度较球蛋白小。伴花生球蛋白的酸解及结构变化程度都小于球蛋白,说明伴花生球蛋白亚基对酸的敏感性低于球蛋白。展开更多
In this work,the content of selenium(Se),physicochemical properties,and antioxidant capacity of Se-enriched peanut proteins isolate(S-PPI)and its fractions arachin(S-Arachin)and conarachin(S-Conarachin)were investigat...In this work,the content of selenium(Se),physicochemical properties,and antioxidant capacity of Se-enriched peanut proteins isolate(S-PPI)and its fractions arachin(S-Arachin)and conarachin(S-Conarachin)were investigated.The S-PPI,S-Arachin,and S-Conarachin were prepared using natural Se-enriched peanut with alkali extraction,acid precipitation,and sedimentation coefficients method.The Se content of S-PPI(420.83μg/kg)was two times compared to ordinary peanut protein isolate(O-PPI,203.10μg/kg).Besides,the Se is more likely to bind with conarachin than arachin.The solubility curves of these peanut proteins at different pH were similar.The emulsifying activities and the emulsion stability of S-Arachin was relatively low,as well as its foaming activity and the foam stability was the lowest.The DPPH scavenging activity of peanut proteins were decreased in order of S-Conarachin,S-PPI,S-Arachin,and O-PPI,as well as reducing power and the superoxide radical scavenging activity.The antioxidant activity trend was similar to Se content distribution trend,suggesting that the content of Se is related to antioxidant activity.The finding may indicate that Se content played a positive role in promoting the antioxidant activity of peanut protein.展开更多
文摘花生球蛋白、伴花生球蛋白及亚基含量显著影响蛋白质的凝胶性和溶解性等功能特性,进而影响其在肉制品、植物蛋白饮料中的应用效果。目前常采用提取蛋白质后再用电泳及光密度法测定球蛋白、伴球蛋白及亚基含量的方法,操作步骤繁琐,样品损失量大。为此收集了178个花生品种,分别提取蛋白,采用电泳法测定球蛋白、伴球蛋白、23.5和37.5 kDa亚基含量并获得大量数据的基础上,利用近红外光谱技术进行整粒花生样品的光谱扫描,将其与传统方法测定的化学值进行拟合,采用偏最小二乘回归(PLSR)化学计量法构建数学模型。通过比较单一和复合光谱预处理方式,对比模型相关系数和误差评估预测模型性能。确定球蛋白模型最佳预处理方法为2^(nd)-der with Detrend,校正集相关系数为0.92,标准差为1.41;伴球蛋白模型最佳预处理方法为Detrend with 1^(st)-der,校正集相关系数为0.85,标准差为1.46;23.5 kDa亚基含量模型最佳预处理方法为Normalization with 2^(nd)-der,校正集相关系数为0.91,标准差为0.53;37.5 kDa模型最佳预处理方法为Detrend with Baseline,校正集相关系数为0.91,标准差为0.89。外部验证结果表明,球蛋白预测均方根误差(square errors of predi ction,SEP)为1.25,伴球蛋白SEP为0.73,23.5 kDa模型SEP为0.47,37.5 kDa模型SEP为0.75。本研究基于近红外光谱技术实现了对整粒花生进行球蛋白、伴球蛋白、23.5 kDa和37.5 kDa亚基含量的同步、快速和无损检测,为育种专家加工专用品种选育和蛋白加工企业原料选用提供了根据。
文摘本文通过Zeta电位、内源荧光光谱、粒度、SDS-PAGE凝胶电泳及溶解性,探讨花生球蛋白和伴花生球蛋白在酸性条件下亚基结构的变化规律。电泳分析表明,花生球蛋白40.5、37.5、35.5和27 ku亚基在常温p H 2.0-3.0的条件下被酸解,产生32.86±0.10ku的新亚基,同时22和15 ku这两条亚基增多;当p H〈2.0时,花生球蛋白的亚基酸解受静电屏蔽抑制。当p H为1.0-3.0,伴花生球蛋白Ⅱ61 ku亚基被酸解产生36.95±0.50、25.14±1.86、18.98±0.78和17.37±1.17 ku这四个条带。进一步研究表明,花生球蛋白和伴花生球蛋白在酸性条件下结构伸展,粒径增大,在p H 2.0-3.0时的Zeta电位及溶解度较高。在p H 2.0-3.0内,花生球蛋白荧光扫描最大发射波长相对中性条件下发生红移,红移幅度大于伴球蛋白,说明伴球蛋白展开程度较球蛋白小。伴花生球蛋白的酸解及结构变化程度都小于球蛋白,说明伴花生球蛋白亚基对酸的敏感性低于球蛋白。
基金supported by the National Natural Science Foundation of China(31301436)Natural Science Fund for Distinguished Young Scholars of Jiangxi Province(20192BCB23006).
文摘In this work,the content of selenium(Se),physicochemical properties,and antioxidant capacity of Se-enriched peanut proteins isolate(S-PPI)and its fractions arachin(S-Arachin)and conarachin(S-Conarachin)were investigated.The S-PPI,S-Arachin,and S-Conarachin were prepared using natural Se-enriched peanut with alkali extraction,acid precipitation,and sedimentation coefficients method.The Se content of S-PPI(420.83μg/kg)was two times compared to ordinary peanut protein isolate(O-PPI,203.10μg/kg).Besides,the Se is more likely to bind with conarachin than arachin.The solubility curves of these peanut proteins at different pH were similar.The emulsifying activities and the emulsion stability of S-Arachin was relatively low,as well as its foaming activity and the foam stability was the lowest.The DPPH scavenging activity of peanut proteins were decreased in order of S-Conarachin,S-PPI,S-Arachin,and O-PPI,as well as reducing power and the superoxide radical scavenging activity.The antioxidant activity trend was similar to Se content distribution trend,suggesting that the content of Se is related to antioxidant activity.The finding may indicate that Se content played a positive role in promoting the antioxidant activity of peanut protein.
