Protein interactions during dry and wet heat pre-treatment of skim milk powder (dispersions) and their effect on the heat stability of recombined filled evaporated milk

Jianfeng Wu; Simin Chen; Els J M Van Damme; Bruno De Meulenaer; Paul Van der Meeren

doi:10.1016/j.foodchem.2023.135974

Protein interactions during dry and wet heat pre-treatment of skim milk powder (dispersions) and their effect on the heat stability of recombined filled evaporated milk

Food Chem. 2023 Aug 30:418:135974. doi: 10.1016/j.foodchem.2023.135974. Epub 2023 Mar 21.

Authors

Jianfeng Wu¹, Simin Chen², Els J M Van Damme², Bruno De Meulenaer³, Paul Van der Meeren⁴

Affiliations

¹ Particle and Interfacial Technology Group (PaInT), Department of Green Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium. Electronic address: Jianfeng.Wu@ugent.be.
² Laboratory of Biochemistry and Glycobiology, Department of Biotechnology, Ghent University, Ghent, Belgium.
³ Department of Food Technology, Safety and Health, Ghent University, Ghent, Belgium.
⁴ Particle and Interfacial Technology Group (PaInT), Department of Green Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium.

PMID: 36965384
DOI: 10.1016/j.foodchem.2023.135974

Abstract

Skim milk powder (SMP) as well as aqueous dispersions were subjected to dry and wet heat pre-treatment, respectively, to improve the heat stability of recombined filled evaporated milk (RFEM) derived therefrom. However, microrheological analysis revealed that prolonged incubation caused detrimental effects on the heat stability of RFEM, which were thought to be due to protein interactions. SDS-PAGE results indicated that protein aggregation via non-disulfide covalent bonds occurred upon long-time dry or wet heat incubation. This was probably related to some Maillard reaction products, which is sustained by the increase in lactulose and protein carbonyl content. Considerable protein aggregation via disulfide bonds in the serum was found upon wet heat incubation at temperatures of at least 80 °C. Principal component analysis (PCA) revealed that the negative effects of overprocessing on the heat stability of RFEM were predominantly related to protein cross-linking via non-disulfide covalent bonds related to protein carbonylation.

Keywords: Dry heating; Heat stability; Protein interaction; Recombined filled evaporated milk; Skim milk powder; Wet heating.

MeSH terms

Animals
Hot Temperature*
Milk Proteins / chemistry
Milk* / chemistry
Powders / analysis
Protein Aggregates
Protein Carbonylation

Substances

Powders
Protein Aggregates
Milk Proteins