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Enhanced Solubility of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation.
Foods ( IF 4.7 ) Pub Date : 2020-06-01 , DOI: 10.3390/foods9060703 Hristo Kalaydzhiev 1 , Radoslav Georgiev 1 , Petya Ivanova 1 , Magdalena Stoyanova 2 , Cristina L M Silva 3 , Vesela I Chalova 1
Foods ( IF 4.7 ) Pub Date : 2020-06-01 , DOI: 10.3390/foods9060703 Hristo Kalaydzhiev 1 , Radoslav Georgiev 1 , Petya Ivanova 1 , Magdalena Stoyanova 2 , Cristina L M Silva 3 , Vesela I Chalova 1
Affiliation
The solubility of plant protein isolates is a key determinant of their potential application. Two protein isolates (PI) from ethanol-treated industrial rapeseed meal, PI10.5–2.5 and PI2.5–8.5, were prepared by sequential isoelectric precipitation of alkali-extracted proteins (pH 12) starting from pH 10.5 to 2.5 or from pH 2.5 to 8.5, respectively. Biochemical analyses revealed that PI2.5–8.5 contained a higher amount of crude protein (72.84%) than PI10.5–2.5 (68.67%). In the same protein isolate, the level of total phenols (0.71%) was almost two-fold higher than that in PI10.5–2.5 (0.42%). No glucosinolates were established in both protein isolates. SDS-PAGE analysis demonstrated that PI10.5–2.5 contained 10 to 15 kDa protein fractions in a relatively higher amount, while PI2.5–8.5 was enriched in 18 to 29 kDa protein fractions. PI10.5–2.5 exhibited high solubility, varying from 41.74% at pH 4.5 to 65.13% at pH 6.5, while PI2.5–8.5 was almost two-fold less soluble under the same conditions. Up to pH 5.5, the addition of NaCl at 0.03 and 0.25 M diminished the solubility of PI2.5–8.5, while the solubility of PI10.5–2.5 was increased. The supplementation of PI10.5–2.5 with 0.25 M NaCl enhanced the protein solubility to 56.11% at pH 4.5 and 94.26% at pH 6.5. The addition of 0.03 M NaCl also increased the solubility of this protein isolate but to a lower extent. Overall, the approach for sequential precipitation of proteins influenced the biochemical characteristics, protein fractional profile and solubility of prepared protein isolates.
中文翻译：
通过顺序等电沉淀制备的菜籽粕分离蛋白的增强溶解度。
植物分离蛋白的溶解度是其潜在应用的关键决定因素。通过从 pH 10.5 至 2.5 或从 pH 2.5 至 pH 12 的碱提取蛋白质 (pH 12) 进行连续等电沉淀，制备了两种来自乙醇处理的工业菜籽粕的分离蛋白 (PI)，PI 10.5–2.5和 PI 2.5–8.5 。分别为8.5。生化分析显示，PI 2.5–8.5的粗蛋白含量 (72.84%) 高于 PI 10.5–2.5 (68.67%)。在同一分离蛋白中，总酚水平 (0.71%) 几乎是 PI 10.5–2.5 (0.42%) 的两倍。在两种蛋白质分离物中均未发现芥子油苷。 SDS-PAGE 分析表明，PI 10.5–2.5含有相对较高含量的 10 至 15 kDa 蛋白质组分，而 PI 2.5–8.5富集 18 至 29 kDa 蛋白质组分。 PI 10.5–2.5表现出高溶解度，从 pH 4.5 时的 41.74% 到 pH 6.5 时的 65.13%，而 PI 2.5–8.5在相同条件下的溶解度几乎低两倍。当 pH 值达到 5.5 时，添加 0.03 和 0.25 M 的 NaCl 会降低 PI 2.5–8.5的溶解度，而增加 PI 10.5–2.5的溶解度。添加 0.25 M NaCl 的 PI 10.5–2.5将蛋白质溶解度在 pH 4.5 时提高至 56.11%，在 pH 6.5 时提高至 94.26%。添加 0.03 M NaCl 也增加了该蛋白质分离物的溶解度，但程度较低。总体而言，蛋白质连续沉淀的方法影响了所制备的蛋白质分离物的生化特性、蛋白质分数谱和溶解度。
更新日期：2020-06-01
中文翻译：
通过顺序等电沉淀制备的菜籽粕分离蛋白的增强溶解度。
植物分离蛋白的溶解度是其潜在应用的关键决定因素。通过从 pH 10.5 至 2.5 或从 pH 2.5 至 pH 12 的碱提取蛋白质 (pH 12) 进行连续等电沉淀，制备了两种来自乙醇处理的工业菜籽粕的分离蛋白 (PI)，PI 10.5–2.5和 PI 2.5–8.5 。分别为8.5。生化分析显示，PI 2.5–8.5的粗蛋白含量 (72.84%) 高于 PI 10.5–2.5 (68.67%)。在同一分离蛋白中，总酚水平 (0.71%) 几乎是 PI 10.5–2.5 (0.42%) 的两倍。在两种蛋白质分离物中均未发现芥子油苷。 SDS-PAGE 分析表明，PI 10.5–2.5含有相对较高含量的 10 至 15 kDa 蛋白质组分，而 PI 2.5–8.5富集 18 至 29 kDa 蛋白质组分。 PI 10.5–2.5表现出高溶解度，从 pH 4.5 时的 41.74% 到 pH 6.5 时的 65.13%，而 PI 2.5–8.5在相同条件下的溶解度几乎低两倍。当 pH 值达到 5.5 时，添加 0.03 和 0.25 M 的 NaCl 会降低 PI 2.5–8.5的溶解度，而增加 PI 10.5–2.5的溶解度。添加 0.25 M NaCl 的 PI 10.5–2.5将蛋白质溶解度在 pH 4.5 时提高至 56.11%，在 pH 6.5 时提高至 94.26%。添加 0.03 M NaCl 也增加了该蛋白质分离物的溶解度，但程度较低。总体而言，蛋白质连续沉淀的方法影响了所制备的蛋白质分离物的生化特性、蛋白质分数谱和溶解度。
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