Department of Chemical Engineering, University of Granada, Granada, Spain.
ISA, Department of Physics and Astronomy, Aarhus University, Aarhus, Denmark.
Food Chem. 2022 Oct 1;390:133169. doi: 10.1016/j.foodchem.2022.133169. Epub 2022 May 8.
The secondary structure of whey protein concentrate hydrolysate (WPCH), used as an emulsifier in oil delivery systems, was investigated using Synchrotron Radiation Circular Dichroism (SRCD). The effect of pH on the conformation of peptides in solution and adsorbed at the oil/water interface, as well as the thermal stability of the systems was studied. Furthermore, oil-loaded microcapsules were produced by spray-drying or electrospraying to investigate the influence of encapsulating agents (glucose syrup, maltodextrin) and drying technique on the secondary structure of WPCH at the oil/water interface. Enzymatic hydrolysis resulted in peptides with a highly unordered structure (∼60% turns and unordered regions) in solution. However, WPCH adsorption onto the oil/water interface increased the α-helical content resulting in an improved thermal stability. The encapsulating agents and spray-drying process did not modify the conformation of WPCH at the oil/water interface. Nonetheless, electrospraying affected the SRCD spectra obtained for WPCH adsorbed at the oil/water interface.
乳清蛋白浓缩物水解物（WPCH）用作油输送系统中的乳化剂，其二级结构使用同步辐射圆二色性（SRCD）进行了研究。研究了 pH 值对溶液中肽和吸附在油/水界面上的肽构象以及体系热稳定性的影响。此外，通过喷雾干燥或静电喷雾制备了含油微胶囊，以研究包埋剂（葡萄糖浆、麦芽糊精）和干燥技术对油/水界面处 WPCH 二级结构的影响。酶解导致溶液中肽的无序结构（约 60%的转角和无规区域）非常高。然而，WPCH 吸附到油/水界面上增加了α-螺旋含量，从而提高了热稳定性。包埋剂和喷雾干燥过程并未改变 WPCH 在油/水界面处的构象。然而，静电喷雾会影响在油/水界面上吸附的 WPCH 的 SRCD 光谱。
