美拉德反应
糖基化
化学
质谱法
基质辅助激光解吸/电离
电喷雾电离
生物化学
色谱法
有机化学
解吸
吸附
受体
标识
DOI:10.1080/10408391003632841
摘要
Protein-reducing sugar conjugates are formed by the naturally occurring Maillard reaction, otherwise known as glycation. The Maillard reaction products (MRP) formed can provide novel and/or improved functionality compared to the unmodified protein. Understanding the chemistry of the Maillard reaction, the physicochemical properties of its products, and, more importantly, the inter-relationships between these properties and the specific functionality of a given MRP will help to define the potential of MRP as food ingredients in their own right. Recently, electrospray ionization-mass spectrometry (ESI-MS) and matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) have acquired a leading role in the structural characterization of proteins. The ability of these techniques to provide detail about the nature and extent of protein modifications at a molecular level as well as conformational information provides new insight into the glycation process. This article reviews the role that ESI- and MALDI-MS have played in advancing our understanding of the glycation of milk proteins.
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