文献类型： 外文期刊

作者： Huan Yang;Zhao yun Cao;Ren xiang Mou;Zhen zhen Cao;Ming xue Chen

作者机构：

期刊名称： Journal of Food Processing and Preservation

ISSN： 0145-8892

年卷期： 2022 年 46 卷 3 期

页码：

收录情况： SCIE（2022版） ; EI（2022版）

摘要： An absolute quantification of α-globulin in rice matrices based on the liquid chromatography–tandem mass spectrometry (LC–MS/MS) utilizing extended stable isotope-labeled (SIL) peptides were studied. Two modified signature peptides, derived from the cysteine-specific modification by IAA during the tryptic digestion process, were identified and selected as the surrogates of α-globulin due to the 1.5–4.5-fold enhancement of intensity peak compared with its unmodified form. The digestion efficiency could be improved from 72.3–98.8% to 94.0–105.3%, and matrix interference normalized from −26.6–4.5% to −6.0–5.5% when the extended SIL peptides were used as ISs. The limit of detection (LOD) and limit of quantification (LOQ) for the α-globulin were 0.25 and 0.8 μg/g, respectively. The recoveries of α-globulin spiked at three levels were between 82 and 105%. The described method was successfully employed for the determination of α-globulin in rice and food product samples. Novelty impact statement: Two modified peptides were selected as surrogates of α-globulin to absolutely quantify the α-globulin allergen in rice based on LC–MS/MS. The extended stable isotope-labeled peptide were used as internal standards to normalize variation from the tryptic digestion and matrix effects. The proposed approach showed excellent sensitivity and accuracy, and successfully applied to determination of the α-globulin in vary rice and food products.

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