Digestibility of Bovine Serum Albumin and Peptidomics of the Digests: Effect of Glycation Derived from α-Dicarbonyl Compounds

α-Dicarbonyl compounds, which are widely generated during sugar fragmentation and oil oxidation, are important precursors of advanced glycation end products (AGEs). In this study, the effect of glycation derived from glyoxal (GO), methylglyoxal (MGO) and diacetyl (DA) on the in vitro digestibility o...

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Bibliographic Details
Published in:Molecules (Basel, Switzerland) Switzerland), 2018-03, Vol.23 (4), p.712
Main Authors: Sheng, Bulei, Larsen, Lotte Bach, Le, Thao T, Zhao, Di
Format: Article
Language:English
Subjects:
advanced glycation end products
Advanced glycosylation end products
Bovine serum albumin
Chemical bonds
Crosslinking
Diacetyl
Digestibility
Electrophoresis
Food science
Gel electrophoresis
glycation
Glycosylation
Intestinal microflora
Intestine
Ionization
Liquid chromatography
Mass spectrometry
Mass spectroscopy
Oxidation
Peptides
Proteins
Pyruvaldehyde
Serum albumin
Small intestine
Sodium
Sodium dodecyl sulfate
α-dicarbonyl compounds
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Summary:α-Dicarbonyl compounds, which are widely generated during sugar fragmentation and oil oxidation, are important precursors of advanced glycation end products (AGEs). In this study, the effect of glycation derived from glyoxal (GO), methylglyoxal (MGO) and diacetyl (DA) on the in vitro digestibility of bovine serum albumin (BSA) was investigated. Glycation from α-dicarbonyl compounds reduced digestibility of BSA in both gastric and intestinal stage of digestion according to measurement of degree of hydrolysis. Changes in peptide composition of digests induced by glycation were displayed, showing absence of peptides, occurrence of new peptides and formation of peptide-AGEs, based on the results obtained using liquid chromatography electron-spray-ionization tandem mass spectrometry (LC-ESI-MS/MS). Crosslinked glycation structures derived from DA largely reduced the sensitivity of glycated BSA towards digestive proteases based on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) results. Network structures were found to remain in the digests of glycated samples by transmission electron microscope (TEM), thus the impact of AGEs in unabsorbed digests on the gut flora should be an interest for further studies.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules23040712