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Proteomic tracking of hydrothermal Maillard and redox modification in lactoferrin and β-lactoglobulin: Location of lactosylation, carboxymethylation and oxidation sites

journal contribution
posted on 2023-05-03, 20:36 authored by Jolon Dyer, Stefan ClerensStefan Clerens, Anita Grosvenor, Ancy ThomasAncy Thomas, Chris Callaghan, Santanu Deb-Choudhury, Stephen HainesStephen Haines
Lactoferrin and β-lactoglobulin are important protein components of mammalian milk. Maillard reactions, as well as redox chemistry, are of particular interest for dairy products because they are known to occur during common processing steps, notably heating procedures such as pasteurization. Using a redox proteomics approach, we characterized AA residue side-chain modification across a range of heating times and with or without the specific addition of lactose, to both map the key modification sites within these proteins and evaluate their sensitivity to process-induced modification. Heating in the presence of lactose resulted in significant Maillard modification (both lactosylation and carboxymethylation) to both bovine lactoferrin and β-lactoglobulin. Notably, Lys47, a key residue in the bioactive peptide lactoferricin, was particularly susceptible to modification. Lactoferrin appeared to be fairly robust to hydrothermal treatment, with relatively low levels of oxidative modification observed. In contrast, β-lactoglobulin was susceptible to significant oxidative modification under hydrothermal treatment, with the range and type of modifications observed suggesting compromised nutritional value. These results have important implications for processing applications in dairy foods where retention of biological function and optimal protein quality is desired.


Rights statement

© American Dairy Science Association®, 2016.


  • English

Does this contain Māori information or data?

  • No


American Dairy Science Association

Journal title

Journal of Dairy Science




Dyer, J. M., Clerens, S., Grosvenor, A., Thomas, A., Callaghan, C., Deb-Choudhury, S., & Haines, S. (2016). Proteomic tracking of hydrothermal Maillard and redox modification in lactoferrin and β-lactoglobulin: location of lactosylation, carboxymethylation and oxidation sites. Journal of Dairy Science, 99(5), 3295-3304. doi: 10.3168/jds.2015-10273

Report number

FBP 56004

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