Kinetic modeling of Maillard and caramelization reactions in sucrose-rich and low moisture foods applied for roasted nuts and seeds


FOOD CHEMISTRY, vol.395, 2022 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 395
  • Publication Date: 2022
  • Doi Number: 10.1016/j.foodchem.2022.133583
  • Journal Name: FOOD CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, PASCAL, Aerospace Database, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Chemical Abstracts Core, Chimica, Communication Abstracts, Compendex, EMBASE, Food Science & Technology Abstracts, MEDLINE, Metadex, Veterinary Science Database, Civil Engineering Abstracts
  • Keywords: Maillard reaction, Caramelization, Kinetic modeling, Roasting, Nuts and seeds, QUANTIFICATION, DEGRADATION, PRODUCTS, LYSINE, RAW, CML, CEL
  • Hacettepe University Affiliated: Yes


A kinetic model was proposed by using a multiresponse kinetic modeling approach for Maillard and caramelization reactions in low moisture foods at neutral pH containing a moderate amount of amino acid and sucrose but a restricted amount reducing sugar. The change in the amount of sucrose, protein-bound lysine, free amino acids, and certain products of Maillard reaction was monitored during roasting of sunflower seed, pumpkin seed, flaxseed, peanut, and almond at 160 and 180 degrees C. A slightly different model was proposed for pumpkin seed due to its difference in compositional and physicochemical characteristics as expressed by principal component analysis. Accordingly, 3-deoxyglucosone formation via sugar degradation; 5-hydroxymethylfurfural formation from 3-deoxyglucosone and only in pumpkin seeds the conversion of N-c-fructoselysine to glyoxal and Heyns product to 1-deoxyglucosone were found to be quantitatively important. N-c-carboxymethyllysine and N-c-carboxyethyllysine mainly originated through oxidation of N-c-fructoselysine and the reaction of methylglyoxal with lysine residue, respectively.