Authentication of leguminous-based products by targeted biomarkers using high resolution time of flight mass spectrometry

Huschek, Gerd; Bönick, Josephine; Merkel, Dietrich; Huschek, Doreen; Rawel, Harshadrai M.

doi:10.1016/j.lwt.2017.12.034

Cited by 17 publications

(13 citation statements)

References 17 publications

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“…For the purpose of cocoa species verification, the extracted proteins and the individual peptides resulting from their tryptic digestion are initially controlled in silico (e.g., using software tools such as Skyline software [ 35 ]) with the BLAST algorithm (Basic Local Alignment Search Tool from the database; UniProt—the Universal Protein Resource: ) as described in [ 36 , 37 ]. The identification then proceeds with help of mass-spectra algorithms and search engines (e.g., Mascot, Matrix Science, London, UK; ) and available databases [ 28 ].…”

Section: Extraction and Classification Of Cocoa Proteinsmentioning

confidence: 99%

“…The discrepancies in protein content observed in the reviewed literature need to be eliminated to obtain more consistent data. The methodical approach using bioinformatics algorithms, targeted peptide biomarkers and high-resolution MS can be recommended here for authentication of the analyzed proteins [ 36 , 37 , 47 ], especially while considering the different aspects of post-harvest processing.…”

Section: Extraction and Classification Of Cocoa Proteinsmentioning

confidence: 99%

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Cocoa Bean Proteins—Characterization, Changes and Modifications due to Ripening and Post-Harvest Processing

et al. 2019

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The protein fractions of cocoa have been implicated influencing both the bioactive potential and sensory properties of cocoa and cocoa products. The objective of the present review is to show the impact of different stages of cultivation and processing with regard to the changes induced in the protein fractions. Special focus has been laid on the major seed storage proteins throughout the different stages of processing. The study starts with classical introduction of the extraction and the characterization methods used, while addressing classification approaches of cocoa proteins evolved during the timeline. The changes in protein composition during ripening and maturation of cocoa seeds, together with the possible modifications during the post-harvest processing (fermentation, drying, and roasting), have been documented. Finally, the bioactive potential arising directly or indirectly from cocoa proteins has been elucidated. The “state of the art” suggests that exploration of other potentially bioactive components in cocoa needs to be undertaken, while considering the complexity of reaction products occurring during the roasting phase of the post-harvest processing. Finally, the utilization of partially processed cocoa beans (e.g., fermented, conciliatory thermal treatment) can be recommended, providing a large reservoir of bioactive potentials arising from the protein components that could be instrumented in functionalizing foods.

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Section: Extraction and Classification Of Cocoa Proteinsmentioning

confidence: 99%

Section: Extraction and Classification Of Cocoa Proteinsmentioning

confidence: 99%

Cocoa Bean Proteins—Characterization, Changes and Modifications due to Ripening and Post-Harvest Processing

et al. 2019

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“…To date, hemp proteins and mass-spectrometry-based methods have not been implemented to study the authentication of complex hemp-containing food products. Previously, LC-MS/MS methods have been developed to detect legume lupine, pea, and soy proteins simultaneously in emulsion-type sausages [ 25 ] and garden pea, meat, and honey in processed vegan or vegetarian food [ 40 ]. The established LODs for soy and lupine isolates or flours were 4 and 2 mg/kg of sausage sample, respectively [ 25 ].…”

Section: Resultsmentioning

confidence: 99%

Multispecies Identification of Oilseed- and Meat-Specific Proteins and Heat-Stable Peptide Markers in Food Products

et al. 2021

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Consumer demand for both plant products and meat products enriched with plant raw materials is constantly increasing. Therefore, new versatile and reliable methods are needed to find and combat fraudulent practices in processed foods. The objective of this study was to identify oilseed species-specific peptide markers and meat-specific markers that were resistant to processing, for multispecies authentication of different meat and vegan food products using the proteomic LC-MS/MS method. To assess the limit of detection (LOD) for hemp proteins, cooked meatballs consisting of three meat species and hemp cake at a final concentration of up to 7.4% were examined. Hemp addition at a low concentration of below 1% was detected. The LOD for edestin subunits and albumin was 0.9% (w/w), whereas for 7S vicilin-like protein it was 4.2% (w/w). Specific heat-stable peptides unique to hemp seeds, flaxseed, nigella, pumpkin, sesame, and sunflower seeds, as well as guinea fowl, rabbit, pork, and chicken meat, were detected in different meat and vegan foods. Most of the oilseed-specific peptides were identified as processing-resistant markers belonging to 11S globulin subunits, namely conlinin, edestin, helianthinin, pumpkin vicilin-like or late embryogenesis proteins, and sesame legumin-like as well as 2S albumins and oleosin isoforms or selected enzymic proteins.

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“…The protein digestion is based on our former reports [44,45]. Briefly, the extracted ATIs were incubated with iodoacetamide for 20 min at 50 °C in the dark to alkylate cleaved disulfide bonds.…”

Section: Methodsmentioning

confidence: 99%

A New Approach of Extraction of α-Amylase/trypsin Inhibitors from Wheat (Triticum aestivum L.), Based on Optimization Using Plackett–Burman and Box–Behnken Designs

et al. 2019

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Wheat is one of the most consumed foods in the world and unfortunately causes allergic reactions which have important health effects. The α-amylase/trypsin inhibitors (ATIs) have been identified as potentially allergen components of wheat. Due to a lack of data on optimization of ATI extraction, a new wheat ATIs extraction approach combining solvent extraction and selective precipitation is proposed in this work. Two types of wheat cultivars (Triticum aestivum L.), Julius and Ponticus were used and parameters such as solvent type, extraction time, temperature, stirring speed, salt type, salt concentration, buffer pH and centrifugation speed were analyzed using the Plackett-Burman design. Salt concentration, extraction time and pH appeared to have significant effects on the recovery of ATIs (p < 0.01). In both wheat cultivars, Julius and Ponticus, ammonium sulfate substantially reduced protein concentration and inhibition of amylase activity (IAA) compared to sodium chloride. The optimal conditions with desirability levels of 0.94 and 0.91 according to the Doehlert design were: salt concentrations of 1.67 and 1.22 M, extraction times of 53 and 118 min, and pHs of 7.1 and 7.9 for Julius and Ponticus, respectively. The corresponding responses were: protein concentrations of 0.31 and 0.35 mg and IAAs of 91.6 and 83.3%. Electrophoresis and MALDI-TOF/MS analysis showed that the extracted ATIs masses were between 10 and 20 kDa. Based on the initial LC-MS/MS analysis, up to 10 individual ATIs were identified in the extracted proteins under the optimal conditions. The positive implication of the present study lies in the quick assessment of their content in different varieties especially while considering their allergenic potential.

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Authentication of leguminous-based products by targeted biomarkers using high resolution time of flight mass spectrometry

Cited by 17 publications

References 17 publications

Cocoa Bean Proteins—Characterization, Changes and Modifications due to Ripening and Post-Harvest Processing

Cocoa Bean Proteins—Characterization, Changes and Modifications due to Ripening and Post-Harvest Processing

Multispecies Identification of Oilseed- and Meat-Specific Proteins and Heat-Stable Peptide Markers in Food Products

A New Approach of Extraction of α-Amylase/trypsin Inhibitors from Wheat (Triticum aestivum L.), Based on Optimization Using Plackett–Burman and Box–Behnken Designs

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