Dataset Information

Simultaneous Mass Spectrometric Detection of Proteins of Ten Oilseed Species in Meat Products.

ABSTRACT: Food fraud is a common issue in the modern food industry. The undeclared use of foreign proteins in meat products is a major concern in this context. Oilseeds are ideal for this purpose due to their high protein content and since huge amounts of oil meal are obtained as a by-product of oil production. Therefore, a UHPLC-MS/MS method was developed for the simultaneous detection of chia, coconut, flaxseed, hemp, peanut, pumpkin, rapeseed, sesame, soy, and sunflower proteins in meat products. Potential tryptic peptide markers were identified by high-resolution mass spectrometry. The final twenty peptide markers selected, which are specific for one of the ten species targeted, were each measured by multiple reaction monitoring. To the best of our knowledge, twelve new heat-stable marker peptides for chia, coconut, flaxseed, pumpkin, rapeseed, sesame and sunflower have not been reported previously. Emulsion-type sausages with 0.01, 0.25, 0.50, 0.75 and 1.00% protein addition by each oilseed species were produced for matrix calibration. No false-positive results were recorded. In the quantification of the ten oilseed species, 466 of 480 measuring data points of the recovery rate in unknown sausages (0.15 and 0.85% protein addition by each oilseed species) were in the accepted range of 80-120%.

SUBMITTER: Sporl J

PROVIDER: S-EPMC9323756 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature

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Simultaneous Mass Spectrometric Detection of Proteins of Ten Oilseed Species in Meat Products.

Spörl Johannes J Speer Karl K Jira Wolfgang W

Foods (Basel, Switzerland) 20220720 14

Food fraud is a common issue in the modern food industry. The undeclared use of foreign proteins in meat products is a major concern in this context. Oilseeds are ideal for this purpose due to their high protein content and since huge amounts of oil meal are obtained as a by-product of oil production. Therefore, a UHPLC-MS/MS method was developed for the simultaneous detection of chia, coconut, flaxseed, hemp, peanut, pumpkin, rapeseed, sesame, soy, and sunflower proteins in meat products. Poten ...[more]

PMID: 35885397

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Project description:Nitroxyl (HNO) exhibits many important pharmacological effects, including inhibition of platelet aggregation, and the HNO donor Angeli's salt has been proposed as a potential therapeutic agent in the treatment of many diseases including heart failure and alcoholism. Despite this, little is known about the mechanism of action of HNO, and its effects are rarely linked to specific protein targets of HNO or to the actual chemical changes that proteins undergo when in contact with HNO. Here we study the presumed major molecular target of HNO within the body: protein thiols. Cysteine-containing tryptic peptides were reacted with HNO, generating the sulfinamide modification and, to a lesser extent, disulfide linkages with no other long lived intermediates or side products. The sulfinamide modification was subjected to a comprehensive tandem mass spectrometric analysis including MS/MS by CID and electron capture dissociation as well as an MS(3) analysis. These studies revealed a characteristic neutral loss of HS(O)NH2 (65 Da) that is liberated from the modified cysteine upon CID and can be monitored by mass spectrometry. Upon storage, partial conversion of the sulfinamide to sulfinic acid was observed, leading to coinciding neutral losses of 65 and 66 Da (HS(O)OH). Validation of the method was conducted using a targeted study of nitroxylated glyceraldehyde-3-phosphate dehydrogenase extracted from Angeli's salt-treated human platelets. In these ex vivo experiments, the sample preparation process resulted in complete conversion of sulfinamide to sulfinic acid, making this the sole subject of further ex vivo studies. A global proteomics analysis to discover platelet proteins that carry nitroxyl-induced modifications and a mass spectrometric HNO dose-response analysis of the modified proteins were conducted to gain insight into the specificity and selectivity of this modification. These methods identified 10 proteins that are modified dose dependently in response to HNO, whose functions range from metabolism and cytoskeletal rearrangement to signal transduction, providing for the first time a possible mechanistic link between HNO-induced modification and the physiological effects of HNO donors in platelets.

Dataset Information

Simultaneous Mass Spectrometric Detection of Proteins of Ten Oilseed Species in Meat Products.

Publications

Simultaneous Mass Spectrometric Detection of Proteins of Ten Oilseed Species in Meat Products.

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