A rapid and simple signature peptides-based method for species authentication of three main commercial Pheretima

2021 ◽  
pp. 104456
Author(s):  
Qiao Liu ◽  
Qirui Bi ◽  
Jingxian Zhang ◽  
Weiwei Qin ◽  
Shanyong Yi ◽  
...  
2019 ◽  
Vol 102 (5) ◽  
pp. 1309-1315
Author(s):  
Jianru Stahl-Zeng ◽  
Ashley Sage ◽  
Philip Taylor ◽  
Jeremy Dietrich Netto ◽  
Tuo Zhang

Abstract Background: Food authenticity is demanded by the consumer at all times. The consumer places trust in the manufacturer that the food product is genuine in terms of what is recorded on the packaging label. Objective: Recent advancements in LC–tandem MS methodology in the detection of allergens, meat, and gelatin speciation in raw food products and processed foods are detailed in this paper. Method: For each of the three methods, initial proteome analysis and the screening leading to the determination of unique tryptic peptides were conducted using a high-resolution, accurate tandem mass spectrometer. Having identified the unique markers, the method was transferred to a tandem quadrupole mass spectrometer for a higher-sensitivity quantitative study, multiple reaction monitoring transition analysis. Results: For the allergens method a detection limit of at least 10 ppm was attained across the 12 allergen peptides in this workflow. In the gluten workflow the resulting chromatograms show good detection down to 5 ppm, with no interference from the food matrices. The meat speciation method details that signature peptides could be readily identified at 1% w/w with no matrix interference. Conclusions: These single-injection workflows with cycle-time optimization enable wide coverage of analytes to identify multiple species within challenging matrix samples.


Trees ◽  
2010 ◽  
Vol 25 (3) ◽  
pp. 465-472 ◽  
Author(s):  
Modhumita Ghosh ◽  
Palanisamy Chezhian ◽  
Ramasamy Sumathi ◽  
Ramasamy Yasodha

2020 ◽  
Author(s):  
Anthony J. Silva ◽  
Rosalee S. Hellberg

Molecules ◽  
2019 ◽  
Vol 24 (10) ◽  
pp. 1920 ◽  
Author(s):  
Yi-Chen Shih ◽  
Jhih-Ting Hsiao ◽  
Fuu Sheu

Stable-isotope dimethyl labeling is a highly reactive and cost-effective derivatization procedure that could be utilized in proteomics analysis. In this study, a liquid chromatography– tandem mass spectrometry in multiple reaction monitoring mode (LC-MS-MRM) platform for the quantification of kiwi allergens was first developed using this strategy. Three signature peptides for target allergens Act d 1, Act d 5, and Act d 11 were determined and were derivatized with normal and deuterated formaldehyde as external calibrants and internal standards, respectively. The results showed that sample preparation with the phenol method provided comprehensive protein populations. Recoveries at four different levels ranging from 72.5–109.3% were achieved for the H-labeled signature peptides of Act d 1 (SPA1-H) and Act d 5 (SPA5-H) with precision ranging from 1.86–9.92%. The limit of quantification (LOQ) was set at 8 pg mL−1 for SPA1-H and at 8 ng mL−1 for SPA5-H. The developed procedure was utilized to analyze seven kinds of hand-made kiwi foods containing 0.0175–0.0515 mg g−1 of Act d 1 and 0.0252–0.0556 mg g−1 of Act d 5. This study extended the applicability of stable-isotope dimethyl labeling to the economical and precise determination of food allergens and peptides.


2019 ◽  
Vol 11 (12) ◽  
pp. 1689-1696 ◽  
Author(s):  
Jingshun Zhang ◽  
Yuwei Hong ◽  
Zengxuan Cai ◽  
Baifen Huang ◽  
Junlin Wang ◽  
...  

A robust UPLC-MS/MS method was established for the quantitative analysis of the major peanut allergens Ara h1 and Ara h2 in baked foodstuffs based on their signature peptides.


PLoS ONE ◽  
2011 ◽  
Vol 6 (3) ◽  
pp. e17812 ◽  
Author(s):  
Li Lian Wong ◽  
Eric Peatman ◽  
Jianguo Lu ◽  
Huseyin Kucuktas ◽  
Shunping He ◽  
...  

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