Structure of milk protein deposits formed by casein micelles and β-lactoglobulin during frontal microfiltration
Structure of milk protein deposits formed by casein micelles and β-lactoglobulin during frontal microfiltration
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DOI：
10.1016/j.memsci.2014.05.027
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发表时间：
2014-10-15
影响因子：
9.5
通讯作者：
Gebhardt, Ronald
中科院分区：
文献类型：
--
作者：
Steinhauer, Tim;Kulozik, Ulrich;Gebhardt, Ronald
采用微滤膜和掠入射小角X射线散射（GISAXS）技术研究了β-乳球蛋白（β-Lg）对酪蛋白胶束（CM）存款结构的影响。过滤实验表明，CM悬浮液的平均比存款阻力随β-Lg浓度的增加而减小。GISAXS用于探测纳米级沉积物的近表面结构。一个核-壳模型用于计算从CM散射显示协议与通过旋涂在硅片上制备的薄膜上的测量。由于β-Lg优先结合在胶束表面，CM的核心变得更加紧凑。微筛过滤沉积物的散射函数表现出质量分形结构的幂律行为特征。这种结构由表面上具有互连的β-Lg分子的密集堆积的CM组成。所得CM网络是多孔的，并解释了在β-Lg存在下平均比存款阻力降低以及渗透流量增加的原因。（C）2014 Elsevier B. V.保留所有权利。
Frontal microfiltration and grazing incidence small angle X-ray scattering (GISAXS) are used to investigate how beta-lactoglobulin (beta-Lg) influences the deposit structure of casein micelles (CM). Filtration experiments show that the mean specific deposit resistance decreases with increasing concentration of beta-Lg in the suspensions of CM. GISAXS is used to probe surface-near structures of deposits on a nano-meter scale. A core-shell model used to compute the scattering from CM shows agreement with measurements on films prepared by spin-coating on silicon wafers. The core of CM becomes more compact as a result of preferential binding of beta-Lg on the micellar surface. Scattering functions of deposits prepared by filtration on micro-sieves show power-law behavior characteristic for mass-fractal structure. This structure consists of dense packed CM with interconnected beta-Lg molecules on the surface. The resulting network of CM is porous and explains the reduced mean specific deposit resistance, as well as the increased permeate flow, in the presence of beta-Lg. (C) 2014 Elsevier B.V. All rights reserved.