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Improvement of emulsifying properties of Maillard reaction products from β
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A novel emulsifier was prepared by conjugating soy β-conglycinin and dextran (MW 67 kDa) under dry-heated Maillard reaction followed by trypsin hydrolysis with the degree of hydrolysis (DH) at 2.2% and 6.5%. The emulsifying properties of β-conglycinin, β-conglycinin–dextran conjugates and hydrolysates of β-conglycinin–dextran conjugates (DH 2.2% and DH 6.5%) were investigated using zeta-potential, droplet size and creaming index of the emulsions. The results showed that hydrolysates of β-conglycinin–dextran conjugates (DH 2.2%) were capable of forming a fine emulsion (d43 = 0.62 ± 0.04 μm, pH 7.0) which remained stable during 4 weeks of storage. A variety of physicochemical and interfacial properties of β-conglycinin, β-conglycinin–dextran conjugates and hydrolysates of β-conglycinin–dextran conjugates were investigated. Hydrolysates of β-conglycinin–dextran conjugates (DH 2.2%) had a much higher fraction of protein adsorption (Fads) and a significantly lower saturation surface load (Γsat) compared with β-conglycinin, β-conglycinin–dextran conjugates and hydrolysates of β-conglycinin–dextran conjugates (DH 6.5%). This might be due to its higher molecular flexibility, which benefited the adsorption and unfolding of peptide molecules at the droplet interface. These might explain its markedly improved emulsifying capability. The conjugation of β-conglycinin and dextran effectively enhanced the hydrophilicity of the oil droplets surfaces and improved the steric repulsion between the oil droplets. Therefore the emulsions were still stable after 4 weeks of storage against pH, ionic strength and thermal treatment. This study demonstrated that controlled enzymatic hydrolysis of protein–polysaccharide conjugates could be an effective method for preparing favourable emulsifiers.
中文翻译：
通过在干热美拉德反应下将大豆 β-伴大豆球蛋白和葡聚糖 (MW 67 kDa) 结合，然后进行胰蛋白酶水解，水解度 (DH) 分别为 2.2% 和 6.5%，制备了一种新型乳化剂。β-伴大豆球蛋白、β-伴大豆球蛋白-葡聚糖偶联物和 β-伴大豆球蛋白-葡聚糖偶联物的水解物（DH 2.2% 和 DH 6.5%）的乳化特性使用乳液的 zeta 电位、液滴大小和乳化指数进行了研究。结果表明，β-伴大豆球蛋白-葡聚糖偶联物（DH 2.2%）的水解物能够形成精细乳液（d43 = 0.62 ± 0.04 μm，pH 7.0），在 4 周的储存期间保持稳定。研究了 β-伴大豆球蛋白、β-伴大豆球蛋白-葡聚糖偶联物和 β-伴大豆球蛋白-葡聚糖偶联物水解物的各种物理化学和界面特性。与β-伴大豆球蛋白、β-伴大豆球蛋白-葡聚糖偶联物和β-伴大豆球蛋白的水解产物相比，β-伴大豆球蛋白-葡聚糖偶联物的水解产物（DH 2.2%）具有更高的蛋白质吸附率（Fads）和显着更低的饱和表面负荷（Γsat） -伴大豆球蛋白-葡聚糖偶联物（DH 6.5%）。这可能是由于其较高的分子灵活性，有利于肽分子在液滴界面处的吸附和展开。这些可能解释了其显着改善的乳化能力。β-伴大豆球蛋白和葡聚糖的共轭作用有效地增强了油滴表面的亲水性并改善了油滴之间的空间排斥。因此，乳液在针对 pH、离子强度和热处理储存 4 周后仍然稳定。 |
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