| 摘要: |
| 为探寻芸豆蛋白加工利用新途径，采用乙酰化处理对芸豆分离蛋白进行改性，通过分析改性过程中芸豆蛋白暴露巯基、游离巯基、二硫键及表面疏水性的变化，探讨乙酰化改性对芸豆分离蛋白凝胶特性的影响。结果表明：1）当乙酸酐与芸豆蛋白质量比为0.2时，蛋白酰化度达到89%，改性过程基本完成，改性后的芸豆分离蛋白在中性条件下（pH6~8）表现出较高的溶解度；2）随乙酰化改性程度的增加，芸豆蛋白总游离巯基的质量摩尔浓度逐渐下降，表面巯基、二硫键的质量摩尔浓度逐渐上升，表面疏水性表现为先下降后上升的趋势。与未改性蛋白相比，乙酰化改性后芸豆分离蛋白的表面巯基的质量摩尔浓度和表面疏水性显著性提高，增强了凝胶形成过程中蛋白质分子相互作用，显著提高了凝胶的硬度、弹性和内聚性。 |
| 关键词: 芸豆分离蛋白 乙酰化 乙酸酐 凝胶特性 |
| DOI：10.11841/j.issn.1007-4333.2018.08.10 |
| 投稿时间：2017-09-02 |
| 基金项目:黑龙江省自然科学基金项目（C2015044）；黑龙江八一农垦大学校内培育课题（XZR2014-10） |
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| Effects of acetylated modification on the gel properties of red kidney bean protein isolation |
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ZUO Feng1, WANG Zhenzhong2, QIAN Lili1, LI Dan1, GUAN Chen1
|
| (1.College of Food Science, Heilongjiang Bayi Agricultural University, Daqing 163319, China;2.China Rural Technology Development Center, Beijing 100045, China) |
| Abstract: |
| To explore new approaches on kidney-bean protein processing,acetylation was utilized to modify kidney bean protein isolate (KPI).The changes of exposed sulfhydryl,free sulfhydryl,disulfide bond and surface hydrophobicity in the process of acetylation were analyzed and then the effects of acetylation on gel properties of KPI were discussed.The results showed that:1) When the ratio of anhydride to protein was 0.2 g/g and acylation degree of protein reached 89%,which means that the modification process was almost completed.Compared with the unmodified KPI,the solubility of modified protein isolate was much higher under neutral condition (pH6-8).2) With the increase of acetylation extent,the total free sulfhydryl molality decreased,the surface sulfhydryl molality and disulfide bond molality gradually increased while surface hydrophobicity displayed the tendency declining at the beginning and rising up in late.Compared with the unmodified KPI,the surface sulfhydryl molality and surface hydrophobicity of modified protein were significant increased,which significantly enhanced the molecular interaction in gel formation process and thus improved the hardness,springiness and cohesiveness of the protein gel. |
| Key words: kidney bean protein isolation acetylated modification acetic anhydride gel properties |
