Effect of glycation derived from a-dicarbonyl compounds on the in vitro digestibility of B-casein and B-lactoglobulin: A model study with glyoxal, methylglyoxal and butanedione

TY - JOUR

T1 - Effect of glycation derived from a-dicarbonyl compounds on the in vitro digestibility of B-casein and B-lactoglobulin: A model study with glyoxal, methylglyoxal and butanedione

AU - Zhao, di

AU - Le, Thao Thi Thu

AU - Larsen, Lotte Bach

AU - Li, Lin

AU - Qin, Dan

AU - Su, Guoying

AU - Li, Bing

PY - 2017/12/1

Y1 - 2017/12/1

N2 - 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.

AB - 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.

KW - Advanced glycation end products

KW - Digestibility

KW - Glycation

KW - α-Dicarbonyl compounds

KW - β-Casein

KW - β-Lactoglobulin

UR - https://www.scopus.com/pages/publications/85042439546

U2 - 10.1016/j.foodres.2017.10.002

DO - 10.1016/j.foodres.2017.10.002

M3 - Journal article

C2 - 29195953

SN - 0963-9969

VL - 102

SP - 313

EP - 322

JO - Food Research International

JF - Food Research International

ER -