Monitoring protein glycation by electrospray ionization (ESI) quadrupole time-of-flight (Q-TOF) mass spectrometer


FOOD CHEMISTRY, vol.217, pp.65-73, 2017 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 217
  • Publication Date: 2017
  • Doi Number: 10.1016/j.foodchem.2016.08.088
  • Journal Name: FOOD CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.65-73
  • Keywords: Protein glycation, Lysozyme, Cytochrome C, beta-casein, Electrospray ionization quadrupole time-of-flight mass spectrometry, BOVINE SERUM-ALBUMIN, MAILLARD REACTION, BETA-LACTOGLOBULIN, QUALITATIVE DETERMINATION, PRODUCTS, MILK, LACTOSE, HEALTH, LYSINE, ENDPRODUCTS
  • Hacettepe University Affiliated: Yes


In this study electrospray ionization quadrupole time-of-flight (ESI-Q-TOF) mass spectrometry was used to investigate protein glycation. The glycated species of cytochrome C, lysozyme, and beta-casein formed during glycation with d-glucose were identified and monitored in binary systems heated at 70 degrees C under dry and aqueous conditions. Cytochrome C had multiple charges in non-glycated state, primarily changing from +13 to +17 positive charges, whereas beta-casein had charge states up to +30. Upon heating with glucose at 70 degrees C in aqueous state, attachment of one glucose molecule onto proteins was observed in each charge state. However, heating in dry state caused much more glucose attachment, leading to the formation of multiple glycoforms of proteins. By using ESI-QTOF-MS technique, formation of glycated cytochrome C containing up to 12 glucose moieties were observed, while glycated species containing 6 and 8 glucose moieties were observed for lysozyme and beta-casein, respectively in various heating conditions. (C) 2016 Elsevier Ltd. All rights reserved.