Development and application of a multiple reaction monitoring mass spectrometry method for absolute quantification of lysinoalanine and lanthionine in dairy products

Document Type

Journal Article

Publication Title

International Dairy Journal

Publisher

Elsevier

School

School of Science

RAS ID

34096

Comments

Nielsen, S. D., Le, T. T., Knudsen, L. J., Rauh, V., Poulsen, N. A., & Larsen, L. B. (2020). Development and application of a multiple reaction monitoring mass spectrometry method for absolute quantification of lysinoalanine and lanthionine in dairy products. International Dairy Journal, 105, Article 104693. https://doi.org/10.1016/j.idairyj.2020.104693

Abstract

Next to the widely studied glycation and Maillard reaction cascade, the heat treatment of milk during production of long shelf-life products may induce side reactions where serine, phosphoserine, glycoserine, cysteine or cystine can be converted into dehydroalanine, which in turn can further react with lysine, histidine or cysteine to yield lysinoalanine (LAL), histidinoalanine (HAL) or lanthionine (LAN) cross-links. The nutritional value, digestibility and functionality of the proteins may be affected by the introduction of covalent cross-links, modified amino acid residues and eventually aggregation. In this study, a liquid chromatography triple quadrupole based method was developed to directly quantify LAL and LAN using multiple reaction monitoring. The method was validated and applied to investigate the content of these cross-links in different dairy products. The level of LAL and LAN was below quantification in raw milk and pasteurised milk, but increasing amounts were measured in ultra-high temperature milk and micellar casein isolate. © 2020 Elsevier Ltd

DOI

10.1016/j.idairyj.2020.104693

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