Effect of glycation derived from α-dicarbonyl compounds on the in vitro digestibility of β-casein and β-lactoglobulin: A model study with glyoxal, methylglyoxal and butanedione. (December 2017)

• Record Type: Journal Article
• Authors: Zhao, Di; Le, Thao T.; Larsen, Lotte Bach; Li, Lin; Qin, Dan; Su, Guoying; Li, Bing
• Is Part Of: Food research international. Volume 102(2017)
• Page Start: 313
• Page End: 322
• Publication Date: 2017-12
• Subjects: α-Dicarbonyl compounds -- Glycation -- Advanced glycation end products -- Digestibility -- β-Casein -- β-Lactoglobulin; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2017.10.002
• Languages: English
• ISSNs: 0963-9969

Abstract

Abstract: α-Dicarbonyl compounds, which are widely found in common consumed food, are one of the precursors of advanced glycation end products (AGEs). In this study, the effect of glycation derived from glyoxal (GO), methylglyoxal (MGO) or butanedione (BU) on the in vitro digestibility of β-casein (β-CN) and β-lactoglobulin (β-Lg) was investigated. Glycation from α-dicarbonyl compounds reduced the in vitro digestibility of studied proteins in both gastric and intestinal stage. In addition, glycation substantially altered the peptides released through gastric and gastrointestinal digestion, as detected by liquid chromatography electrospray-ionization tandem mass spectrometry (LC-ESI-MS/MS). Crosslinked glycation structures derived from BU considerably reduced the sensitivity of glycated β-Lg towards digestive proteases, albeit to a lesser degree in glycated β-CN due to its intrinsic unordered structure. By contrast, non-crosslinked AGEs that formed adjacent to enzymatic cleavage sites did not block the enzymatic reaction in several cases, as evidenced by the corresponding digested peptides modified with glycation structures. These findings expand our understanding of the nutritional influence of α-dicarbonyl compounds and health impact of relevant dietary AGEs. Graphical abstract: Highlights: Glycation reduced gastric digestibility and altered gastric digested peptides. Gastric and gastrointestinal digested peptides profiles were substantially changed by glycation. Glycation showed less influence on β-CN digestibility due to its intrinsic disordered structure. Non-crosslinked AGEs affect the digestion process to a lesser extent than crosslinked ones.