Moscovici Alice M, Joubran Yousef, Briard-Bion Valerie, Mackie Alan, Dupont Didier, Lesmes Uri
Department of Biotechnology and Food Engineering, Technion - Israel Institute of Technology, Haifa 32000, Israel.
Food Funct. 2014 Aug;5(8):1898-908. doi: 10.1039/c4fo00248b.
The Maillard reaction has been proposed as a natural pathway to functionalize proteins and modulate their proteolysis. Nevertheless, gaps in understanding the digestive fate of Maillard reaction products (MRPs) still exist, especially regarding bioactive proteins such as lactoferrin (LF). UV absorbance and SDS-PAGE were used to monitor reaction progression under mild thermal processing (60 °C, 79% RH). Dynamic light scattering showed that MRPs had increased colloidal size and turbidity at 3 < pH < 10. FRAP analysis and in vitro digestion experiments demonstrated that MRPs possessed improved antioxidant capacity and higher susceptibility to proteolysis to varying extents under adult conditions compared to infant conditions. Proteomic analyses of MRP digesta revealed altered enzymatic cleavage patterns with no pronounced changes in the formation of known bioactive peptides. These also indicated that MRPs may breakdown in the gastro-intestinal tract to potentially form novel bioactive peptides. Overall, this work highlights that the Maillard reaction could be harnessed to modify the extent of proteolysis and bioactivity of proteins.
美拉德反应已被提出作为一种使蛋白质功能化并调节其蛋白水解的天然途径。然而，在理解美拉德反应产物（MRPs）的消化命运方面仍存在差距，尤其是对于乳铁蛋白（LF）等生物活性蛋白。在温和热处理（60°C，79%相对湿度）条件下，使用紫外吸光度和SDS-PAGE监测反应进程。动态光散射表明，在3<pH<10时，MRPs的胶体尺寸和浊度增加。FRAP分析和体外消化实验表明，与婴儿条件相比，在成人条件下，MRPs具有更高的抗氧化能力，并且在不同程度上对蛋白水解的敏感性更高。对MRP消化物的蛋白质组学分析显示，酶切模式发生了改变，已知生物活性肽的形成没有明显变化。这些结果还表明，MRPs可能在胃肠道中分解，潜在地形成新的生物活性肽。总体而言，这项工作强调了美拉德反应可用于改变蛋白质的蛋白水解程度和生物活性。
