College of Food Science and Engineering , Tianjin University of Science & Technology, State Key Laboratory of Food Nutrition and Safety , No. 29 The Thirteenth Road, Tianjin Economy and Technology Development Area , Tianjin 300457 , P. R. China.
Tianjin Key Laboratory of Food Science and Health, School of Medicine , Nankai University , Tianjin 300071 , P. R. China.
J Agric Food Chem. 2019 Sep 25;67(38):10734-10743. doi: 10.1021/acs.jafc.9b04337. Epub 2019 Sep 16.
Glutenin is the main protein of flour and is a very important source of protein nutrition for humans. Methylglyoxal (MGO) is an important product of the Maillard reaction that occurs during the hot-processing of flour products, and it reacts with glutenin to facilitate changes in glutenin properties. Here, the effects of MGO on glutenin digestion during the heating process were investigated using a simulated MGO-glutenin system. MGO significantly reduced the digestibility of glutenin. The structure of MGO-glutenin and physicochemical properties were studied to understand the mechanism of the decrease of digestibility. These data suggest that changes in digestibility were caused by decreases in surface hydrophobicity and increases in disulfide bonds. MGO induces strong aggregation of glutenin after heating that led to the masking of cleavage sites for proteases. Moreover, carbonyl oxidation induced by MGO leads to intermolecular cross-linking of glutenin that increasingly masks or even destroys cleavage sites, further decreasing digestibility.
谷蛋白是面粉中的主要蛋白质，是人类蛋白质营养的重要来源。甲基乙二醛（MGO）是面粉制品热加工过程中发生的美拉德反应的重要产物，它与谷蛋白反应，促进谷蛋白性质的变化。在这里，使用模拟的 MGO-谷蛋白系统研究了 MGO 对加热过程中谷蛋白消化的影响。MGO 显著降低了谷蛋白的消化率。研究了 MGO-谷蛋白的结构和物理化学性质，以了解消化率降低的机制。这些数据表明，消化率的变化是由于表面疏水性降低和二硫键增加引起的。MGO 在加热后诱导谷蛋白强烈聚集，从而掩盖蛋白酶的切割位点。此外，MGO 诱导的羰基氧化导致谷蛋白分子间交联，越来越多地掩盖甚至破坏切割位点，进一步降低消化率。
