Dairy products and the Maillard reaction: A promising future for extensive food characterization by integrated proteomics studies

被引:93
作者
Arena, Simona [1 ]
Renzone, Giovanni [1 ]
D'Ambrosio, Chiara [1 ]
Salzano, Anna Maria [1 ]
Scaloni, Andrea [1 ]
机构
[1] CNR, Prote & Mass Spectrometry Lab, ISPAAM, Via Argine 1085, I-80147 Naples, Italy
关键词
Milk; Maillard reaction; Heating; Lactosylation; Advanced-glycation end-products; Oxidation; PERFORMANCE LIQUID-CHROMATOGRAPHY; ADVANCED GLYCATION ENDPRODUCTS; TANDEM MASS-SPECTROMETRY; BETA-LACTOGLOBULIN MODIFICATIONS; MILK-PROTEINS; HEAT-TREATMENT; KAPPA-CASEIN; PROCESSED MILK; WHEY PROTEINS; MODEL SYSTEMS;
D O I
10.1016/j.foodchem.2016.09.165
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Heating of milk and dairy products is done using various technological processes with the aim of preserving microbiological safety and extending shelf-life. These treatments result in chemical modifications in milk proteins, mainly generated as a result of the Maillard reaction. Recently, different bottom-up proteomic methods have been applied to characterize the nature of these structural changes and the modified amino acids in model protein systems and/or isolated components from thermally-treated milk samples. On the other hand, different gel-based and shotgun proteomic methods have been utilized to assign glycation, oxidation and glycoxidation protein targets in diverse heated milks. These data are essential to rationalize eventual, different nutritional, antimicrobial, cell stimulative and antigenic properties of milk products, because humans ingest large quantities of corresponding thermally modified proteins on a daily basis and these molecules also occur in pharmaceuticals and cosmetics. This review provides an updated picture of the procedures developed for the proteomic characterization of variably-heated milk products, highlighting their limits as result of concomitant factors, such as the multiplicity and the different concentration of the compounds to be detected. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码:477 / 489
页数:13
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