Determination of osteocalcin in meat and bone meal of bovine and porcine origin using matrix-assisted laser desorption ionization/time-of-flight mass spectrometry and high-resolution hybrid mass spectrometry

Balizs, Gabor; Weise, Christoph; Rozycki, Christel; Opialla, Tobias; Sawada, Stefanie; Zagon, Jutta; Lampen, Alfonso

doi:10.1016/j.aca.2011.03.027

Cited by 24 publications

(9 citation statements)

References 23 publications

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“…The main alternative biomolecules that have been widely investigated as a source of species information are proteins, which are coded for by DNA and therefore contain less albeit some level of genetic information useful for species determination. Early protein-based methods were based on immunological techniques [ 25 , 26 ], which continue to be developed and utilised by some [ 27 , 28 ], but the increasing use of protein sequence-based methods, particularly following the development of soft-ionization mass spectrometry in the late 1980s and technical improvements in the 1990s resulting in the emerging field of proteomics, has been so far more widely utilised in the fields of bioarchaeology [ 29 , 30 ] and microbial studies [ 31 , 32 ] than in the animal feed industry (although note [ 33 ]).…”

Section: Molecular Techniques In Species Identificationmentioning

confidence: 99%

Species Identification of Bovine, Ovine and Porcine Type 1 Collagen; Comparing Peptide Mass Fingerprinting and LC-Based Proteomics Methods

Buckley

2016

IJMS

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Collagen is one of the most ubiquitous proteins in the animal kingdom and the dominant protein in extracellular tissues such as bone, skin and other connective tissues in which it acts primarily as a supporting scaffold. It has been widely investigated scientifically, not only as a biomedical material for regenerative medicine, but also for its role as a food source for both humans and livestock. Due to the long-term stability of collagen, as well as its abundance in bone, it has been proposed as a source of biomarkers for species identification not only for heat- and pressure-rendered animal feed but also in ancient archaeological and palaeontological specimens, typically carried out by peptide mass fingerprinting (PMF) as well as in-depth liquid chromatography (LC)-based tandem mass spectrometric methods. Through the analysis of the three most common domesticates species, cow, sheep, and pig, this research investigates the advantages of each approach over the other, investigating sites of sequence variation with known functional properties of the collagen molecule. Results indicate that the previously identified species biomarkers through PMF analysis are not among the most variable type 1 collagen peptides present in these tissues, the latter of which can be detected by LC-based methods. However, it is clear that the highly repetitive sequence motif of collagen throughout the molecule, combined with the variability of the sites and relative abundance levels of hydroxylation, can result in high scoring false positive peptide matches using these LC-based methods. Additionally, the greater alpha 2(I) chain sequence variation, in comparison to the alpha 1(I) chain, did not appear to be specific to any particular functional properties, implying that intra-chain functional constraints on sequence variation are not as great as inter-chain constraints. However, although some of the most variable peptides were only observed in LC-based methods, until the range of publicly available collagen sequences improves, the simplicity of the PMF approach and suitable range of peptide sequence variation observed makes it the ideal method for initial taxonomic identification prior to further analysis by LC-based methods only when required.

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Section: Molecular Techniques In Species Identificationmentioning

confidence: 99%

Species Identification of Bovine, Ovine and Porcine Type 1 Collagen; Comparing Peptide Mass Fingerprinting and LC-Based Proteomics Methods

Buckley

2016

IJMS

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“…Furthermore, the use of stable isotope labeled standard peptides allows a quantification of peptides by measuring peptide ratios. This technique offers the possibility for species identification and quantification in highly processed samples such as PAPs. , While the application of mass spectrometry (MS) for meat authentication within the field of food chemistry is well established, − in feed authentication, it has not yet been widely applied. ,− Recently, Marbaix et al used targeted MS to set up an assay for three bovine peptides derived from hemoglobin α and heat shock protein β-1 with the capability to detect ruminant PAP in vegetal feed with a limit of detection of 5% …”

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confidence: 99%

Mass Spectrometry-Based Immunoassay for the Quantification of Banned Ruminant Processed Animal Proteins in Vegetal Feeds

Steinhilber

Schmidt

Naboulsi³

et al. 2018

Anal. Chem.

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The ban of processed animal proteins (PAPs) in feed for farmed animals introduced in 2001 was one of the main EU measures to control the bovine spongiform encephalopathy (BSE) crisis. Currently, microscopy and polymerase chain reaction (PCR) are the official methods for the detection of illegal PAPs in feed. However, the progressive release of the feed ban, recently with the legalization of nonruminant PAPs for the use in aquaculture, requires the development of alternative methods to determine the species origin and the source (legal or not). Additionally, discussions about the need for quantitative tests came up, particularly if the zero-tolerance-concept is replaced by introducing PAP thresholds. To address this issue, we developed and partially validated a multiplex mass spectrometry-based immunoassay to quantify ruminant specific peptides in vegetal cattle feed. The workflow comprises a new sample preparation procedure based on a tryptic digestion of PAPs in suspension, a subsequent immunoaffinity enrichment of the released peptides, and a LC-MS/MS-based analysis for peptide quantification using isotope labeled standard peptides. For the very first time, a mass spectrometry-based method is capable of detecting and quantifying illegal PAPs in animal feed over a concentration range of 4 orders of magnitude with a detection limit in the range of 0.1% to 1% (w/w).

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“…Also proteomics studies focussing on food authenticity were already successfully performed [17,[27][28][29][30]. However few were applied to PAP [24,31,32]. In most cases standard bottom-up proteomics workflows were used as means to correctly identify the samples of interest.…”

Section: Introductionmentioning

confidence: 99%

Species and tissues specific differentiation of processed animal proteins in aquafeeds using proteomics tools

Rasinger¹,

Marbaix

Dieu

et al. 2016

Journal of Proteomics

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Determination of osteocalcin in meat and bone meal of bovine and porcine origin using matrix-assisted laser desorption ionization/time-of-flight mass spectrometry and high-resolution hybrid mass spectrometry

Cited by 24 publications

References 23 publications

Species Identification of Bovine, Ovine and Porcine Type 1 Collagen; Comparing Peptide Mass Fingerprinting and LC-Based Proteomics Methods

Species Identification of Bovine, Ovine and Porcine Type 1 Collagen; Comparing Peptide Mass Fingerprinting and LC-Based Proteomics Methods

Mass Spectrometry-Based Immunoassay for the Quantification of Banned Ruminant Processed Animal Proteins in Vegetal Feeds

Species and tissues specific differentiation of processed animal proteins in aquafeeds using proteomics tools

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