Two soy protein 11S fractions with different surface sulfhydryl contents were prepared.Utilizing analytical ultracentrifugation,the effects of storage time and hydrogen peroxide at different concentrations(0.5-100 mmo...Two soy protein 11S fractions with different surface sulfhydryl contents were prepared.Utilizing analytical ultracentrifugation,the effects of storage time and hydrogen peroxide at different concentrations(0.5-100 mmol/L)on the two 11S fractions were investigated.Results show that after removing 2-mercaptoethanol(2-ME)by size exclusion chromatography,the 11S fraction with high surface sulfhydryl content(2.0 mol sulfhydryl/mol 11S)progressively formed 15S and 21S in dilute solutions during storage at 4℃ for 82 days.While,the 11s fraction with low surface sulfhydryl content(0.2 mol sulfhydryl/mol 11S)was stable under the same condition.Moreover,after treating the 11s with high surface sulfhydryl content with 1 mmol/L H_(2)O_(2),the weight percentage of 15S reached the maximum value of 20%.The 15S induced by air and H_(2)O_(2)could be totally converted to 11S with the addition of 10 mmol/L 2-ME,which could be attributed to that the disulfide bond linking two 11S molecules is on the surface of the 15S and easily accessible to the reducing agent 2-ME.This study helps us to deeply understand the formation mechanism of 15S and the stability of 11S.展开更多
大豆贮藏蛋白主要成分是7S和11S球蛋白,大豆贮藏蛋白组分及其亚基组成决定了蛋白质的品质和加工特性。本研究选用134对细胞核SSR标记,对166份栽培大豆微核心种质进行基因分型,运用一般线性回归(general linear model,GLM)和复合线性回归...大豆贮藏蛋白主要成分是7S和11S球蛋白,大豆贮藏蛋白组分及其亚基组成决定了蛋白质的品质和加工特性。本研究选用134对细胞核SSR标记,对166份栽培大豆微核心种质进行基因分型,运用一般线性回归(general linear model,GLM)和复合线性回归(mixed linear model,MLM)方法进行标记与性状的关联分析,定位大豆蛋白亚基的相关基因。结果表明,2年均检测到的且与蛋白亚基相关联的SSR位点有14个,以MLM方法检测到5个SSR位点(Sat_062、Satt583、Satt291、Satt234和Satt595)与蛋白亚基相关联;7S组分各亚基变异程度较大,是引起11S/7S变异的主要原因;表型变异较大的亚基可能因为相关基因进化中发生重组较多,LD衰减距离较小,导致检测到较少的相关位点。本研究结果对蛋白亚基相关性状的标记辅助选择育种有重要的利用价值。展开更多
基金supported by the National Natural Science Foundation of China(No.22173092 and No.21674107).
文摘Two soy protein 11S fractions with different surface sulfhydryl contents were prepared.Utilizing analytical ultracentrifugation,the effects of storage time and hydrogen peroxide at different concentrations(0.5-100 mmol/L)on the two 11S fractions were investigated.Results show that after removing 2-mercaptoethanol(2-ME)by size exclusion chromatography,the 11S fraction with high surface sulfhydryl content(2.0 mol sulfhydryl/mol 11S)progressively formed 15S and 21S in dilute solutions during storage at 4℃ for 82 days.While,the 11s fraction with low surface sulfhydryl content(0.2 mol sulfhydryl/mol 11S)was stable under the same condition.Moreover,after treating the 11s with high surface sulfhydryl content with 1 mmol/L H_(2)O_(2),the weight percentage of 15S reached the maximum value of 20%.The 15S induced by air and H_(2)O_(2)could be totally converted to 11S with the addition of 10 mmol/L 2-ME,which could be attributed to that the disulfide bond linking two 11S molecules is on the surface of the 15S and easily accessible to the reducing agent 2-ME.This study helps us to deeply understand the formation mechanism of 15S and the stability of 11S.
文摘大豆贮藏蛋白主要成分是7S和11S球蛋白,大豆贮藏蛋白组分及其亚基组成决定了蛋白质的品质和加工特性。本研究选用134对细胞核SSR标记,对166份栽培大豆微核心种质进行基因分型,运用一般线性回归(general linear model,GLM)和复合线性回归(mixed linear model,MLM)方法进行标记与性状的关联分析,定位大豆蛋白亚基的相关基因。结果表明,2年均检测到的且与蛋白亚基相关联的SSR位点有14个,以MLM方法检测到5个SSR位点(Sat_062、Satt583、Satt291、Satt234和Satt595)与蛋白亚基相关联;7S组分各亚基变异程度较大,是引起11S/7S变异的主要原因;表型变异较大的亚基可能因为相关基因进化中发生重组较多,LD衰减距离较小,导致检测到较少的相关位点。本研究结果对蛋白亚基相关性状的标记辅助选择育种有重要的利用价值。
