Quantification of advanced glycation end products and amino acid cross-links in foods by high-resolution mass spectrometry: Applicability of acid hydrolysis

被引:36
作者
Akillioglu, Halise Gul [1 ]
Lund, Marianne N. [1 ,2 ]
机构
[1] Univ Copenhagen, Fac Sci, Dept Food Sci, Rolighedsvej 26, DK-1958 Frederiksberg, Denmark
[2] Univ Copenhagen, Fac Hlth & Med Sci, Dept Biomed Sci, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark
关键词
Advanced glycation end-products; Hydrophilic interaction liquid chromatography; High resolution mass spectrometry; Amino acid crosslinks; Acid stability; MAILLARD REACTION-PRODUCTS; EPSILON-CARBOXYMETHYL-LYSINE; ENDPRODUCTS AGES; CHROMATOGRAPHY; FUROSINE; LYSINOALANINE; LANTHIONINE; INDICATORS; PROTEINS; SERUM;
D O I
10.1016/j.foodchem.2021.130601
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
An analytical method was developed and validated for simultaneous identification and quantification of advanced glycation end products (AGEs), amino acid cross-links, lysine and arginine in foodstuffs based on acid hydrolysis, hydrophilic interaction chromatography and high-resolution mass spectrometry. The method proved to be sensitive, reproducible and accurate for furosine, N-epsilon-(carboxymethyDlysine, N-epsilon-(carboxyethyDlysine, methylglyoxal and glyoxal-derived hydroimidazolones (MG-H and GO-H isomers, respectively), glyoxal lysine dimer, lysinoalanine, lanthionine, lysine and arginine. LOD and LOQ values in water were found to be 0.9-15.5 ng/mL and 2.8-47 ng/mL, respectively, and increased to 1.4-60 ng/mL and 4.4-182 ng/mL in liquid infant formula. Recovery values ranged from 76 to 118% in four different food matrices. Microwave-assisted hydrolysis for 11 min had similar efficiency as conventional hydrolysis, which requires overnight incubation. Acid stability of each compound was determined during microwave and conventional hydrolysis, and showed that the MG-H1 isomer is partially converted to the MG-H3 isomer during acid hydrolysis.
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页数:10
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共 43 条
[1]  
Ahmed N, 2002, BIOCHEM J, V364, P1
[2]   Advanced glycation endproducts - role in pathology of diabetic complications [J].
Ahmed, N .
DIABETES RESEARCH AND CLINICAL PRACTICE, 2005, 67 (01) :3-21
[3]   Lactose hydrolysis and protein fortification pose an increased risk for the formation of Maillard reaction products in UHT treated milk products [J].
Aktag, Isil Gursul ;
Hamzalioglu, Aytul ;
Gokmen, Vural .
JOURNAL OF FOOD COMPOSITION AND ANALYSIS, 2019, 84
[4]   Digestibility of extruded proteins and metabolic transit of Nε-carboxymethyllysine in rats [J].
Alamir, Issam ;
Niquet-Leridon, Celine ;
Jacolot, Philippe ;
Rodriguez, Camille ;
Orosco, Martine ;
Anton, Pauline M. ;
Tessier, Frederic J. .
AMINO ACIDS, 2013, 44 (06) :1441-1449
[5]   Analysis of Chemically Labile Glycation Adducts in Seed Proteins: Case Study of Methylglyoxal-Derived Hydroimidazolone 1 (MG-H1) [J].
Antonova, Kristina ;
Vikhnina, Maria ;
Soboleva, Alena ;
Mehmood, Tahir ;
Heymich, Marie-Louise ;
Leonova, Tatiana ;
Bankin, Mikhail ;
Lukasheva, Elena ;
Gensberger-Reigl, Sabrina ;
Medvedev, Sergei ;
Smolikova, Galina ;
Pischetsrieder, Monika ;
Frolov, Andrej .
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2019, 20 (15)
[6]   Analysis of advanced glycation endproducts in dairy products by isotope dilution liquid chromatography-electrospray tandem mass spectrometry. The particular case of carboxymethyllysine [J].
Delatour, Thierry ;
Hegele, Joerg ;
Parisod, Veronique ;
Richoz, Janique ;
Maurer, Sarah ;
Steven, Matthew ;
Buetler, Timo .
JOURNAL OF CHROMATOGRAPHY A, 2009, 1216 (12) :2371-2381
[7]   Forty years of furosine - Forty years of using Maillard reaction products as indicators of the nutritional quality of foods [J].
Erbersdobler, Helmut F. ;
Somoza, Veronika .
MOLECULAR NUTRITION & FOOD RESEARCH, 2007, 51 (04) :423-430
[8]   Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins [J].
Friedman, M .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1999, 47 (04) :1295-1319
[9]   Isolation and characterization of glyoxal-arginine modifications [J].
Glomb, MA ;
Lang, G .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2001, 49 (03) :1493-1501
[10]   Amides are novel protein modifications formed by physiological sugars [J].
Glomb, MA ;
Pfahler, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (45) :41638-41647