Evidence map›Paper›PMID 37780262›Full record

ArticleFood chemistry: X2023

Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry.

Hannah McKerchar, Jolon M Dyer, Juliet A Gerrard, Evelyne Maes, Stefan Clerens, Renwick C J Dobson

Open access · goldAbstract read
In one paragraph

Article in Food chemistry: X, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Protein Extraction from Mealworm (Foods (Basel, Switzerland) · 2026
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 5 institutions in 2 countries.

Hannah McKercharBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand.
Jolon M DyerBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand.
Juliet A GerrardBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand.
Evelyne MaesBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand.
Stefan ClerensBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand.
Renwick C J DobsonBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand.
Riddet Institute · NZAgResearch · NZLincoln University · NZMassey University · NZUniversity of Canterbury · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Food processingLysinoalanineMass spectrometryProtein–protein crosslinks

Identifiers

PMID37780262
PMCPMC10534164
OpenAlexW4385154949

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.