Optimization of MALDI-TOF mass spectrometry imaging for the visualization and comparison of peptide distributions in dry-cured ham muscle fibers

Maslov, Dina Rešetar; Svirkova, Anastasiya; Allmaier, Günter; Marchetti-Deschamann, Martina; Pavelić, Sandra Kraljević

doi:10.1016/j.foodchem.2018.12.126

Cited by 38 publications

(27 citation statements)

References 68 publications

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“…Although the identification of proteins by mass spectrometry of peptide fragments has been performed extensively using MALDI-MS, there are a few examples of peptide evaluation in food compared with studies of lipids and carbohydrates. The localization of peptides in food has been analyzed in a variety of food including crabs, [49], fishes [79], prawns [92], peaches [94], tomatoes [95], and hams [71,80,81] (Table 3). Denaturation of proteins and peptides has been shown to negatively affect the nutritional, sensory, and quality characteristics of cooked ham.…”

Section: Proteins and Peptidesmentioning

confidence: 99%

Application of Mass Spectrometry Imaging for Visualizing Food Components

Yoshimura

Zaima

2020

Foods

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Consuming food is essential for survival, maintaining health, and triggering positive emotions like pleasure. One of the factors that drive us toward such behavior is the presence of various compounds in foods. There are many methods to analyze these molecules in foods; however, it is difficult to analyze the spatial distribution of these compounds using conventional techniques, such as mass spectrometry combined with high-performance liquid chromatography or gas chromatography. Mass spectrometry imaging (MSI) is a two-dimensional ionization technology that enables detection of compounds in tissue sections without extraction, purification, separation, or labeling. There are many methods for ionization of analytes, including secondary ion mass spectrometry, matrix-assisted laser desorption/ionization, and desorption electrospray ionization. Such MSI technologies can provide spatial information on the location of a specific analyte in food. The number of studies utilizing MSI technologies in food science has been increasing in the past decade. This review provides an overview of some of the recent applications of MSI in food science and related fields. In the future, MSI will become one of the most promising technologies for visualizing the distribution of food components and for identifying food-related factors by their molecular weights to improve quality, quality assurance, food safety, nutritional analysis, and to locate administered food factors.

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Section: Proteins and Peptidesmentioning

confidence: 99%

Application of Mass Spectrometry Imaging for Visualizing Food Components

Yoshimura

Zaima

2020

Foods

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“…The identification of peptides generated during proteolysis of dry-cured ham has been of high interest during the last decade and the obtained results have been used for a better understanding of the phenomena as well as to characterize the potential bioactivity or functional activity that many of these peptides could exert [ 8 ]. Up to date, the main methodologies used were based on peptidomic strategies using electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) ionization techniques coupled to mass spectrometry in tandem (MS/MS) [ 12 , 13 ]. The data analysis of the obtained spectra for the identification of the peptide sequence was frequently carried out using search engines such as Mascot and protein databases (i.e., UniProt, NCBInr), and a list of peptide sequences as well as their origin proteins were obtained according to a score value.…”

Section: Introductionmentioning

confidence: 99%

Identification and Quantitation of Bioactive and Taste-Related Dipeptides in Low-Salt Dry-Cured Ham

Heres

Gallego

2022

IJMS

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The reduction of salt in meat products influences the natural mechanisms of proteolysis occurring in their processing, and could affect the final characteristics of the product in terms of texture and flavor due to its effect on the activity of enzymes. In the present study, the quantitation of dipeptides PA, GA, VG, EE, ES, DA, and DG in low-salt Spanish dry-cured ham was carried out using a triple quadrupole mass spectrometry instrument. The developed methodology demonstrated the advantages of hydrophilic interaction liquid chromatography in the removal of salt as a clean-up/separation step before ionization. This resulted in a value of 44.88 μg/g dry-cured ham for GA dipeptide, and values ranging from 2 to 8 μg/g dry-cured ham for VG, EE, ES, DA, and DG dipeptides. PA showed the lowest concentration with a value of 0.18 μg/g dry-cured ham. These outcomes prove the remarkable activity of muscular dipeptidyl peptidases during dry-curing as well as confirming the presence of these dipeptides which are related to certain taste attributes (e.g., ‘bitter’ or ‘umami’). Such dipeptides have also been confirmed as anti-inflammatory and potential cardiovascular protectors using in vitro assays, with the advantage of dipeptides small size increases their chance to resist both gastrointestinal digestion and intestinal/bloodstream transport without being degraded or modified.

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“…Imaging mass spectrometry (IMS) is a technology that enables the mapping of hundreds to thousands of molecules within biological systems. − The instruments within the field can measure a diverse array of sample types and chemical classes, ranging from low molecular weight metabolites − and signaling molecules − to lipids, − peptides, − and proteins. − A typical IMS experiment involves defining an area of the sample surface to be imaged followed by the desorption and ionization at multiple discrete locations. Each desorbed location, or pixel, is composed of an individual mass spectrum.…”

Section: Introductionmentioning

confidence: 99%

Multimodal Imaging Mass Spectrometry: Next Generation Molecular Mapping in Biology and Medicine

Neumann

Djambazova

Caprioli

et al. 2020

J. Am. Soc. Mass Spectrom.

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Imaging mass spectrometry has become a mature molecular mapping technology that is used for molecular discovery in many medical and biological systems. While powerful by itself, imaging mass spectrometry can be complemented by the addition of other orthogonal, chemically informative imaging technologies to maximize the information gained from a single experiment and enable deeper understanding of biological processes. Within this review, we describe MALDI, SIMS, and DESI imaging mass spectrometric technologies and how these have been integrated with other analytical modalities such as microscopy, transcriptomics, spectroscopy, and electrochemistry in a field termed multimodal imaging. We explore the future of this field and discuss forthcoming developments that will bring new insights to help unravel the molecular complexities of biological systems, from single cells to functional tissue structures and organs.

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Optimization of MALDI-TOF mass spectrometry imaging for the visualization and comparison of peptide distributions in dry-cured ham muscle fibers

Cited by 38 publications

References 68 publications

Application of Mass Spectrometry Imaging for Visualizing Food Components

Application of Mass Spectrometry Imaging for Visualizing Food Components

Identification and Quantitation of Bioactive and Taste-Related Dipeptides in Low-Salt Dry-Cured Ham

Multimodal Imaging Mass Spectrometry: Next Generation Molecular Mapping in Biology and Medicine

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