Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry
Formation of lysinoalanine protein–protein crosslinks during food processing adversely impacts nutritional value. However, mapping lysinoalanine directly in food is challenging. We characterized the fragmentation pattern of lysinoalanine crosslinks in synthetic peptide models over a range of pH and...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-10-01
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| Series: | Food Chemistry: X |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157523002432 |
| _version_ | 1797676590832812032 |
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| author | Hannah McKerchar Jolon M. Dyer Juliet A. Gerrard Evelyne Maes Stefan Clerens Renwick C.J. Dobson |
| author_facet | Hannah McKerchar Jolon M. Dyer Juliet A. Gerrard Evelyne Maes Stefan Clerens Renwick C.J. Dobson |
| author_sort | Hannah McKerchar |
| collection | DOAJ |
| description | Formation of lysinoalanine protein–protein crosslinks during food processing adversely impacts nutritional value. However, mapping lysinoalanine directly in food is challenging. We characterized the fragmentation pattern of lysinoalanine crosslinks in synthetic peptide models over a range of pH and time treatments using mass spectrometry. A putative diagnostic ion resulting from the cleavage of the α-carbon and β-carbon of lysinoalanine is identified in MALDI MS/MS spectra. This represents the first step in mapping lysinoalanine in real food samples with higher precision than currently identifiable through standard or customized software. We then determined a correlated trend in the reduction of disulfide bonds and formation of lysinoalanine with increasing pH and time. Mapping lysinoalanine formation is critical to enhance our understanding of molecular processes impacting the nutritional value of foods, including notably in the development of protein alternatives that use alkaline treatment to extract protein isolates. |
| first_indexed | 2024-03-11T22:31:27Z |
| format | Article |
| id | doaj.art-f5ee742fdad84a6795bbf9fda2e60a23 |
| institution | Directory Open Access Journal |
| issn | 2590-1575 |
| language | English |
| last_indexed | 2024-03-11T22:31:27Z |
| publishDate | 2023-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: X |
| spelling | doaj.art-f5ee742fdad84a6795bbf9fda2e60a232023-09-23T05:12:19ZengElsevierFood Chemistry: X2590-15752023-10-0119100800Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometryHannah McKerchar0Jolon M. Dyer1Juliet A. Gerrard2Evelyne Maes3Stefan Clerens4Renwick C.J. Dobson5Biomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand; Riddet Institute, Based Massey University, Palmerston North 4442, New Zealand; Proteins and Metabolites Team, AgResearch Lincoln Research Centre, Lincoln 7608, New ZealandBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand; The New Zealand Institute for Plant and Food Research, Lincoln Research Centre, Lincoln 7608, New Zealand; Department of Wine, Food and Molecular Biosciences, Lincoln University, Lincoln 7647, New ZealandBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand; Riddet Institute, Based Massey University, Palmerston North 4442, New Zealand; School of Biological Sciences and School of Chemical Sciences, University of Auckland, Auckland, New ZealandBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand; Riddet Institute, Based Massey University, Palmerston North 4442, New Zealand; Proteins and Metabolites Team, AgResearch Lincoln Research Centre, Lincoln 7608, New ZealandBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand; Riddet Institute, Based Massey University, Palmerston North 4442, New Zealand; Proteins and Metabolites Team, AgResearch Lincoln Research Centre, Lincoln 7608, New ZealandBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand; Riddet Institute, Based Massey University, Palmerston North 4442, New Zealand; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Victoria 3010, Australia; Corresponding author at: School of Biological Sciences, University of Canterbury, Private Bag 4800, Christchurch 8140, New Zealand.Formation of lysinoalanine protein–protein crosslinks during food processing adversely impacts nutritional value. However, mapping lysinoalanine directly in food is challenging. We characterized the fragmentation pattern of lysinoalanine crosslinks in synthetic peptide models over a range of pH and time treatments using mass spectrometry. A putative diagnostic ion resulting from the cleavage of the α-carbon and β-carbon of lysinoalanine is identified in MALDI MS/MS spectra. This represents the first step in mapping lysinoalanine in real food samples with higher precision than currently identifiable through standard or customized software. We then determined a correlated trend in the reduction of disulfide bonds and formation of lysinoalanine with increasing pH and time. Mapping lysinoalanine formation is critical to enhance our understanding of molecular processes impacting the nutritional value of foods, including notably in the development of protein alternatives that use alkaline treatment to extract protein isolates.http://www.sciencedirect.com/science/article/pii/S2590157523002432LysinoalanineProtein–protein crosslinksFood processingMass spectrometry |
| spellingShingle | Hannah McKerchar Jolon M. Dyer Juliet A. Gerrard Evelyne Maes Stefan Clerens Renwick C.J. Dobson Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry Food Chemistry: X Lysinoalanine Protein–protein crosslinks Food processing Mass spectrometry |
| title | Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry |
| title_full | Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry |
| title_fullStr | Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry |
| title_full_unstemmed | Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry |
| title_short | Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry |
| title_sort | characterizing lysinoalanine crosslinks in food systems discovery of a diagnostic ion in model peptides using maldi mass spectrometry |
| topic | Lysinoalanine Protein–protein crosslinks Food processing Mass spectrometry |
| url | http://www.sciencedirect.com/science/article/pii/S2590157523002432 |
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