Department of Food Science, University of Wisconsin, Madison 53706.
Department of Food Science, University of Wisconsin, Madison 53706.
J Dairy Sci. 2021 Apr;104(4):3916-3926. doi: 10.3168/jds.2020-18311. Epub 2021 Feb 19.
The solubility of high-protein milk protein concentrate (MPC) may decrease significantly during storage, particularly at relatively high temperatures and humidity. The objective of this study was to seek correlations between the solubility loss of MPC during storage and various surface characteristics determined on the basis of simultaneous nanoscale topographical imaging and nanomechanical mapping of MPC particle surfaces using atomic force microscopy. A control MPC and a calcium-depleted MPC were stored at 45°C and 66% relative humidity for up to 60 d. The solubility of the control MPC was 56% at the beginning of the storage and gradually decreased to 10% at the end of the 60-d storage. The calcium-depleted MPC exhibited more rapid decreases from almost 100% at the beginning of the storage to 18% after storage for 45 d, after which we observed no significant difference in solubility between the control and calcium-depleted MPC. Averaged or root mean squared roughness values calculated using topographical images were found to have no correlation with the solubility. Deformation, Derjaguin-Muller-Toropov modulus, and adhesion images revealed the presence of individual casein micelles and larger clusters of aggregated casein micelles at MPC particle surfaces, whereas we observed no correlation between the solubility and averaged values of these nanomechanical properties. Furthermore, Derjaguin-Muller-Toropov modulus and adhesion images showed that the peripheral edges of individual casein micelles and their clusters had significantly higher values of the corresponding nanomechanical properties than other regions in the images, indicating the occurrence of the fusion of casein micelles. The surface area coverage or the percent area of the fused regions in an image revealed significant negative linear correlations with the solubility for both the control and calcium-depleted MPC. The present results support the hypothesis that the fusion of casein micelles at MPC powder particle surfaces is a causative factor for the solubility loss of MPC during storage and in turn suggest that the solubility loss may be alleviated by inhibiting the formation of a crust or skin on powder particle surfaces.
高蛋白牛奶蛋白浓缩物(MPC)在储存过程中的溶解度可能会显著下降,特别是在相对较高的温度和湿度下。本研究的目的是寻求 MPC 在储存过程中溶解度损失与基于原子力显微镜对 MPC 颗粒表面进行纳米级形貌成像和纳米力学映射所确定的各种表面特性之间的相关性。对照 MPC 和钙耗竭 MPC 在 45°C 和 66%相对湿度下储存长达 60 天。对照 MPC 的溶解度在储存开始时为 56%,逐渐下降到储存结束时的 10%。钙耗竭 MPC 在储存开始时几乎从 100%迅速下降到 45 天储存后的 18%,之后我们观察到对照 MPC 和钙耗竭 MPC 之间的溶解度没有显著差异。使用形貌图像计算的平均或均方根粗糙度值与溶解度没有相关性。变形、德加古因-米勒-托波洛夫模量和粘附图像显示,在 MPC 颗粒表面存在单个酪蛋白胶束和更大的聚集酪蛋白胶束簇,而我们观察到这些纳米力学特性的平均值与溶解度之间没有相关性。此外,德加古因-米勒-托波洛夫模量和粘附图像显示,单个酪蛋白胶束及其簇的外围边缘具有明显更高的相应纳米力学特性值,表明酪蛋白胶束发生了融合。图像中融合区域的表面积覆盖率或百分比与对照 MPC 和钙耗竭 MPC 的溶解度均呈现显著的负线性相关。本研究结果支持了以下假说,即 MPC 粉末颗粒表面上的酪蛋白胶束融合是 MPC 在储存过程中溶解度损失的一个原因,并暗示通过抑制粉末颗粒表面结皮或表皮的形成,可能缓解溶解度损失。