| Autor: |
Lotte J. Knudsen, Valentin Rauh, Jannik N. Pedersen, Peter Dekker, Daniel E. Otzen, Lotte B. Larsen, Søren D-H. Nielsen |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
|
| Zdroj: |
Journal of Dairy Science, Vol 107, Iss 12, Pp 10497-10511 (2024) |
| Druh dokumentu: |
article |
| ISSN: |
0022-0302 |
| DOI: |
10.3168/jds.2024-25103 |
| Popis: |
ABSTRACT: During processing and storage of both conventional and lactose-hydrolyzed UHT milk (LHM), aggregation of milk proteins occurs. Protein aggregation can inter alia occur via nonreducible covalent cross-links derived from either Maillard or dehydroalanine (DHA) pathways. To study this further in relation to processing method and lactase enzyme purity, LHM was produced using 3 different lactase preparations, with lactase enzymes added in a dairy setting either before (prehydrolysis) or after (posthydrolysis) UHT treatment. The prepared LHM types were subsequently stored at either 25°C or 35°C for up to one year. Mass spectrometry was used to absolutely quantify the level of furosine, N-ε-(carboxymethyl)lysine, N-ε-(carboxyethyl)lysine, lanthionine, and lysinoalanine in these products using a newly developed method on triple quadrupole for these processing-induced markers. The results showed higher levels of Maillard-related processing markers in prehydrolyzed LHM compared with posthydrolyzed LHM and conventional UHT milk, which, on the other hand, contained higher concentrations of DHA-derived cross-links. Proteomics of collected particles from asymmetrical flow field-flow fractionation in combination with gel electrophoresis indicated the presence of intramicellar cross-links during storage, especially for larger particles involving αS1- and αS2-caseins. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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