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

Zhao, Di; Le, Thao T.; Larsen, Lotte Bach; Li, Lin; Qin, Dan; Su, Guoying

doi:10.1016/j.foodres.2017.10.002

Cited by 63 publications

(79 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Peptides 2, 4, 5, 7 and 8 contained glycated Lys (K) which were not cleaved by proteases. These results correspond to the previous finding that glycated Lys of Arg will not be selected by trypsin . The activity site of trypsin selectively acts on Lys and Arg since their ϵ‐amino groups or guanido groups are positively charged.…”

Section: Resultssupporting

confidence: 90%

“…pyrraline) or even reverse (e.g. CML) the positive charges of Lys and Arg, thus removing the trypsin‐sensitive sites . In addition, peptides 2, 5, 7 and 8 contain unglycated Lys (K) or Arg (R) residues other than glycated ones.…”

Section: Resultsmentioning

confidence: 99%

“…Glycation also changes the digestion behavior of proteins, which is related to its nutritional value. Most studies have revealed that glycation reduces the susceptibility of glycated proteins to proteolysis by blocking Lys and Arg residues in the intestinal digestion . Preferential glycation sites in β ‐Lg (Lys 47 , Lys 60 , Lys 75 , Lys 77 , Lys 83 , Lys 91 , Lys 100 , Lys 135 and Lys 138 ), β ‐CN (Lys 113 , Lys 169 and Lys 176 ) and BSA (Lys 12 , Lys 76 , Lys 221 , Lys 224 , Lys 232 , Lys 294 , Lys 312 , Lys 322 and Lys 377 ) have been identified using proteomics methods .…”

Section: Introductionmentioning

confidence: 99%

“…Although there have been many studies reporting the digestibility of glycated milk protein, most have focused on measuring degree of hydrolysis (DH), showing sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) images of digests. Detailed information on the digests such as the composition of peptides and glycation information have only been revealed in a few studies . The peptide composition after digestion of a protein is closely related to its nutrition value, bioactivity and effects on gut flora .…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Zhao

et al. 2019

J Sci Food Agric

Self Cite

View full text Add to dashboard Cite

BACKGROUND Milk proteins are widely used in food production and are often glycated by reducing sugar. Although many studies have reported the digestibility of glycated milk protein, most have focused on measuring degree of hydrolysis (DH), showing sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) image of digests. Detailed information on the changes in peptide composition of digests has seldom been revealed. Therefore, in addition to measuring the DH and showing the SGS‐PAGE images of digests, we also analyzed the peptidomics in digests using liquid chromatography–electrospray ionization–tandem mass spectrometry (LC‐ESI‐MS/MS) and Mascot database in this work to further reveal the influence of glycation on protein nutrition. RESULTS Compared with β‐lactoglobulin and bovine serum albumin (BSA), DH of β‐casein was suppressed to a lesser extent by glycation in both gastric and intestinal stages. Aggregates of glycated BSA were less sensitive to the action of digestive enzymes throughout gastrointestinal digestion according to SDS‐PAGE images. Changes in the peptide composition of digests induced by glycation were distinctly displayed, showing both absence of peptides and occurrence of new peptides, based on the results obtained from LC‐ESI‐MS/MS. CONCLUSIONS Glycation can greatly change the peptide composition in digests of milk protein. The nutritional impact of the change in the peptide composition requires further investigation, and the impact of MRPs in unabsorbed digests on the gut flora should be an interesting field for further studies. © 2018 Society of Chemical Industry

show abstract

Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Zhao

et al. 2019

J Sci Food Agric

Self Cite

View full text Add to dashboard Cite

show abstract

“…Combination of -dicarbonyls and amino compounds generate various glycation structures, such as N( )-carboxymethyl-lysine (CML), GO-derived hydroimidazolone (G-H), N( )-carboxyethyl-lysine (CEL), MGO-derived hydroimidazolone (MG-H) and pyrraline. [8][9][10] Glycation by reducing sugars have been widely reported to change aggregation behavior of proteins by changing both covalent and non-covalent interactions during heat treatment.…”

Section: Introductionmentioning

confidence: 99%

Heat‐induced amyloid‐like aggregation of β‐lactoglobulin affected by glycation by α‐dicarbonyl compounds in a model study

Zhao

Zhang

et al. 2019

J Sci Food Agric

Self Cite

View full text Add to dashboard Cite

BACKGROUND α‐Dicarbonyl compounds are widely generated in the Maillard reaction, caramelization and oil oxidation during heat treatment. These compounds can readily react with lysine and arginine residues of a protein, whereas the influence of these compounds on protein structure and quality has seldom been revealed. This study compared influence of glycation by glucose and α‐dicarbonyl compounds on amyloid‐like aggregation of β‐lactoglobulin (β‐LG), both fibrillation kinetics and conformation of aggregates were studied. RESULTS Compared with glycation by glucose, the glycation by α‐dicarbonyl compounds resulted in faster reduction of free amino group, sulfydryl group, and the relative content of β‐sheet secondary structure, according to the ultraviolet (UV) spectra or circular dichroism (CD) spectra results. Based on the analysis of fibrillation kinetics using thioflavin T (ThT) binding assay, the glycation by α‐dicarbonyls were more efficient in suppressing the growth of fibrillar aggregates. In addition, glycation by α‐dicarbonyl resulted in amorphous oligomers, which were compared with the amyloid‐like aggregates in control and glucose‐glycated samples, based on the transmission electron microscopy (TEM) observation. CONCLUSIONS Glycation by α‐dicarbonyl compounds induced larger decline in the β‐sheet structure of β‐LG than glycation by glucose, and thus largely suppressed the amyloid‐like aggregation of β‐LG and changed the morphology of aggregates. © 2019 Society of Chemical Industry

show abstract

Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing

Dong

et al. 2021

Food Science & Nutrition

View full text Add to dashboard Cite

α‐Dicarbonyl compounds (α‐DCs) are a class of compounds generated during the thermal processing of food. Due to the high reactivity, α‐DCs were endowed with the ability to react with food components thus lowering nutrition value and even leading to a potential risk for food safety. In this study, methylglyoxal (MG), the most abundant α‐DCs, was selected to investigate the alteration effects on the structure and digestibility of α‐lactalbumin (αLA) under thermal processing (60–100°C). The results showed that the modification degree of αLA by MG increased with the rise of processing temperature, accompanied by the significant changes in molecular weight, intrinsic fluorescence, and secondary structures of αLA. High‐resolution mass spectrometry analysis identified that lysine (Lys) and arginine (Arg) are the modification sites, and Nε‐(carboxyethyl)‐L‐lysine is the main modification type. Since the Lys and Arg are also the cleavage sites of trypsin, the digestibility of MG modified αLA (MG‐αLA) by trypsin correspondingly decreased with an increase of processing temperature. The reacted Lys and Arg residues, and the protein‐bound AGEs were quantified, and the contents were found to be highly dependent on the temperature.

show abstract

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

Cited by 63 publications

References 45 publications

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Heat‐induced amyloid‐like aggregation of β‐lactoglobulin affected by glycation by α‐dicarbonyl compounds in a model study

Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing

Contact Info

Product

Resources

About