Improving the functional properties of soy glycinin by enzymatic treatment. Adsorption and foaming characteristics
Improving the functional properties of soy glycinin by enzymatic treatment. Adsorption and foaming characteristics
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DOI：
10.1016/j.foodhyd.2008.03.011
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发表时间：
2009-03
影响因子：
10.7
通讯作者：
V. P. Ruiz-Henestrosa;C. Sánchez;J. Pedroche;F. Millán;J. Patino
中科院分区：
文献类型：
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作者：
V. P. Ruiz-Henestrosa;C. Sánchez;J. Pedroche;F. Millán;J. Patino
在这方面的贡献，我们已经确定了有限的酶水解的影响，对界面（动态吸附和表面吸附性能）和起泡（泡沫形成和稳定）的大豆球蛋白（大豆球蛋白，馏分11 S）的特性。水解度（DH= 0%、2%和6%）、水溶液的pH（pH=5和7）和溶液中的蛋白质浓度（0.1、0.5和1wt%）是研究的变量。温度和离子强度分别保持恒定在20°C和0.05M。大豆球蛋白在空气-水界面上的吸附速率和表面吸附性质（表面吸附模量、E和损耗角）取决于pH和DH。吸附急剧下降，在pH值为5.0，接近等电点的大豆球蛋白，因为存在一个滞后期和低速率的扩散。大豆球蛋白的界面特性通过酶处理大大改善，特别是在酸性水溶液的情况下。具有低DH的水解产物具有改善的功能特性（主要是发泡能力和泡沫稳定性），尤其是在接近等电点（pI）的pH下，因为天然蛋白质在pH = pI下更难以在流体界面处转化成膜。泡沫容量取决于蛋白质扩散到界面的速率，并且通过酶处理大大提高。泡沫稳定性与表面压力相关，在很小程度上，与长期吸附的表面膨胀模量相关，很少有例外。
In this contribution we have determined the effect of limited enzymatic hydrolysis on the interfacial (dynamics of adsorption and surface dilatational properties) and foaming (foam formation and stabilization) characteristics of a soy globulin (glycinin, fraction 11S). The degree of hydrolysis (DH=0%, 2%, and 6%), the pH of the aqueous solution (pH=5 and 7), and the protein concentration in solution (at 0.1, 0.5 and 1wt%) were the variables studied. The temperature and the ionic strength were maintained constant at 20°C and 0.05M, respectively. The rate of adsorption and surface dilatational properties (surface dilatational modulus, E, and loss angle) of glycinin at the air–water interface depend on the pH and DH. The adsorption decreased drastically at pH 5.0, close to the isoelectric point of glycinin, because of the existence of a lag period and a low rate of diffusion. The interfacial characteristics of glycinin are much improved by enzymatic treatment, especially in the case of acidic aqueous solutions. Hydrolysates with a low DH have improved functional properties (mainly foaming capacity and foam stability), especially at pH close to the isoelectric point (pI), because the native protein is more difficult to convert into a film at fluid interfaces at pH≈pI. The foam capacity depends on the rate of diffusion of protein to the interface and is much improved by the enzymatic treatment. Foam stability correlates with surface pressure and, to a minor extent, with surface dilatational modulus at long-term adsorption with few exceptions.