巯基乙醇对大豆分离蛋白热致聚合物界面性质的影响

董世荣; 王丽; 姜丙焱; 徐微

doi:10.13386/j.issn1002-0306.2020070331

巯基乙醇对大豆分离蛋白热致聚合物界面性质的影响

doi: 10.13386/j.issn1002-0306.2020070331

董世荣^1,,
王丽²,
姜丙焱¹,
徐微^1, ,

1.
哈尔滨学院食品工程学院, 食品生物技术重点实验室，黑龙江哈尔滨 150086
2.
济南市第二药品不良反应监测中心，山东济南 271100

基金项目: 国家自然科学基金（31801485）；省级大学生创新创业训练计划支持项目（202010234052，202010234061）；哈尔滨学院青年博士科研启动基金项目（HUDF2019204），黑龙江省自然科学基金（LH2020C064）

详细信息

作者简介:
董世荣（1988−），女，博士研究生，研究方向：蛋白质修饰、纳米颗粒制备，E-mail：dongshirong118@126.com

通讯作者:
徐微（1982−），女，博士研究生，研究方向：蛋白质构效关系及植物资源的开发利用，E-mial：xweihappy@163.com

中图分类号: TS201.2
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出版历程
- 收稿日期: 2020-07-28
- 网络出版日期: 2021-04-08

The Effect of Mercaptoethanol on the Interface Properties of Heat-Induced Aggregation of Soy protein Isolate

1.
School of Food Engineering, Key Laboratory of Food Biotechnology, Harbin University, Harbin 150086)
2.
The Jinan second Center for Adverse Drug Reaction Monitoring, Jinan 271100

摘要

摘要: 为探讨β-巯基乙醇对大豆分离蛋白热致聚合物界面性质的影响，以大豆分离蛋白为原料，在pH7.0、90 ℃加热添加和不添加β-巯基乙醇（2 mmol/L）的浓度为10 mg/mL大豆分离蛋白溶液0 h和10 h，制备不同大豆分离蛋白质热致聚合物。观察了大豆分离蛋白、添加β-巯基乙醇大豆分离蛋白、大豆分离蛋白热致聚合物和β-巯基乙醇大豆分离蛋白热致聚合物的微观形态、游离巯基含量的变化，同时比较了起泡能力、泡沫稳定性、乳化活性、乳化稳定性、表面疏水性和浊度的差异。结果表明，大豆分离蛋白和添加β-巯基乙醇大豆分离蛋白呈现无规则状态，大豆分离蛋白热致聚合物为有规则的球状颗粒，而β-巯基乙醇大豆分离蛋白热致聚合物部分形成球状聚合物部分形成无规则聚合物。添加β-巯基乙醇改善了大豆分离蛋白的界面性质。与大豆分离蛋白相比较，添加β-巯基乙醇大豆分离蛋白和添加β-巯基乙醇大豆分离蛋白热致聚合物的起泡能力分别提高了64.56%和95.77%，乳化活性提高的幅度分别为12.94%和14.61%。添加β-巯基乙醇大豆分离蛋白和添加β-巯基乙醇大豆分离蛋白热致聚合物在长时间储藏中表现出良好的乳化稳定性和泡沫稳定性。这种良好的界面性质源于β-巯基乙醇的加入赋予聚合物具有更高的游离巯基含量和表面疏水性。并且本实验建立了4种样品的泡沫稳定性和乳化稳定性随时间变化的Rational函数和Linear函数经验模型，为大豆分离蛋白质的实际应用奠定了理论基础。
- 大豆分离蛋白 /
- β-巯基乙醇 /
- 聚合物 /
- 起泡性 /
- 乳化性
Abstract: In ordert oinvestigate the effect of β-mercaptoethanol onthe interface properties of soy protein isolate(SPI), the samples (10 mg/mL) were prepared by heating with or without β-mercaptoethanol (2 mmol/L) at pH7.0 and 90 ^oC for 0 h and 10 h. The micromorphology and free sulfhydryl group of the samples were observed. Meanwhile, the foaming ability, foam stability, emulsifying activity, emulsifying stability, surface hydrophobicity and turbidity were evaluated. The results showed that irregular aggregations were formed from SPI and SPI with β-mercaptoethanol. The regular spherical particles were formed from SPI by heating, while both regular spherical particles and irregular aggregations were formed from SPI with β-mercaptoethanol by heating. The interface properties of SPI were improved by adding β-mercaptoethanol. Compared with those of SPI, the foaming abilities of SPI with β-mercaptoethanol and the aggregations formed from SPI with β-mercaptoethanol increased by 64.56% and 95.77%, respectively. Moreover, their emulsifying activities increased by 12.94% and 14.61%, respectively. Good emulsifying stability and foam stability of SPI with β-mercaptoethanol and the aggregations formed from SPI with β-mercaptoethanol were found during long time storage. The reason for the good interfacial property was that the higher free sulfhydryl content and surface hydrophobicity of SPI and its aggregations were obtained by the addition of β-mercaptoethanol. The empirical models of Rational function and Linear function of foam stability and emulsion stability for the 4 samples with time were established, which laid a theoretical foundation for the practical application of SPI.
- soy protein isolate /
- β-mercaptoethanol /
- aggregations /
- foaming property /
- emulsifying property

HTML全文

图 1 4种聚合物微观形态图

注：a：大豆分离蛋白，b：β巯基乙醇大豆分离蛋白，c：大豆分离蛋白热致聚合物，d：β-巯基乙醇大豆分离蛋白热致聚合物；图3、图4、图6同。

Figure 1. The transmission electron micrographs for the four aggregations

下载: 全尺寸图片幻灯片

图 2 4种聚合物起泡性的变化

注：a：起泡能力，b：泡沫稳定性。

Figure 2. The foam properties of soy protein and its aggregates

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图 3 归一化的大豆分离蛋白和2种聚合物的泡沫稳定性回归分析结果

Figure 3. Regressed results of generalized foam stability of soy protein and their aggregations with time by least-square fitting

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图 4 4种聚合物泡沫静置1min和10min时微观形态图（40×40）

Figure 4. The foam micrograph of the four samples at 1 minand 10 min（40×40）

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图 5 4种聚合物的乳化性的变化

注：a：乳化活性，b：乳化稳定性。

Figure 5. The emulsifying properties of soy protein isolate and their aggregates

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图 6 归一化大豆分离蛋白和大豆分离蛋白聚合物乳化稳定性回归分析结果

Figure 6. Regressed results of generalized emulsifying stability of soy protein isolate and their aggregations with time by least-square fitting

下载: 全尺寸图片幻灯片

图 7 不同样品浊度的变化(660 nm)

Figure 7. The turbidity (at 660 nm) of soy protein and their aggregations

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表 1 天然大豆分离蛋白和热致聚合物游离巯基含量的变化

Table 1. The change of free sulfhydryl group for the soyprotein isolate and their heating induced aggregations

样品	游离巯基含量（μmol/g）
大豆分离蛋白	21.38±0.77^a
β-巯基乙醇大豆分离蛋白	50.87±1.01^c
大豆分离蛋白热致聚合物	6.04±0.45^b
β-巯基乙醇大豆分离蛋白热致聚合物	51.23±0.89^c
注：小写字母相同表示差异不显著，不同字母表示差异显著（P<0.05）；表2同。

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表 2 4种样品表面疏水性的变化

Table 2. The change of surface hydrophobicity for thefour samples

样品	表面疏水性（S_o）
大豆分离蛋白	276.96±5.64^a
β-巯基乙醇大豆分离蛋白	950.87±8.01^c
大豆分离蛋白热致聚合物	853.48±9.87^b
β-巯基乙醇大豆分离蛋白热致聚合物	1012.23±11.28^d

下载: 导出CSV

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