The Experts below are selected from a list of 1482 Experts worldwide ranked by ideXlab platform

Jennifer A Sealeyvoyksner - One of the best experts on this subject based on the ideXlab platform.

  • novel aspects of quantitation of immunogenic wheat gluten peptides by liquid chromatography mass spectrometry mass spectrometry
    Journal of Chromatography A, 2010
    Co-Authors: Jennifer A Sealeyvoyksner, Chaitan Khosla, Robert D Voyksner, James W Jorgenson
    Abstract:

    Abstract A novel, specific and sensitive non-immunological liquid chromatography–mass spectrometry (LC–MS) based assay has been developed to detect and quantify trace levels of wheat gluten in food and consumer products. Detection and quantification of dietary gluten is important, because gluten is a principle trigger of a variety of immune diseases including food allergies and intolerances. One such disease, celiac sprue, can cause intestinal inflammation and enteropathy in patients who are exposed to dietary gluten. At present, immunochemistry is the leading analytical method for gluten detection in food. Consequently, enzyme-linked immunosorbent assays (ELISAs), such as the sandwich or competitive type assays, are the only commercially available methods to ensure that food and consumer products are accurately labeled as gluten-free. The availability of a comprehensive, fast and economic alternative to the immunological ELISA may also facilitate research towards the development of new drugs, therapies and food processing technologies to aid patients with gluten intolerances and for gluten-free labeling and certification purposes. LC–MS is an effective and efficient analytical technique for the study of Cereal Grain Proteins and to quantify trace levels of targeted dietary gluten peptides in complex matrices. Initial efforts in this area afforded the unambiguous identification and structural characterization of six unique physiologically relevant wheat gluten peptides. This paper describes the development and optimization of an LC–MS/MS method that attempts to provide the best possible accuracy and sensitivity for the quantitative detection of trace levels of these six peptides in various food and consumer products. The overall performance of this method was evaluated using native Cereal Grains. Experimental results demonstrated that this method is capable of detecting and quantifying select target peptides in food over a range from 10 pg/mg to 100 ng/mg (corresponding to approximately 0.01–100 ppm). Limits of detection (LOD) and quantification (LOQ) for the six target peptides were determined to range from 1 to 30 pg/mg and 10–100 pg/mg respectively. Reproducibility of the assay was demonstrated by evaluation of calibration data as well as data collected from the analysis of quality control standards over a period of four consecutive days. The average coefficient of determination (R2) for each peptide was consistently found to be >0.995 with residuals ranging from approximately 80% to 110%. Spike recovery data for each peptide in various matrices was evaluated at a concentration level near the approximate LOQ for each, as well as at higher concentration levels (30 and 60 ng/mg). The average range of accuracy of detection for all peptides at the lower concentration level was determined to be 90% (±11), while accuracy at the 30 and 60 ng/mg levels was 98% (±5%) and 98% (±3%), respectively. The usefulness and capabilities of this method are presented in a practical application to prospectively screen a variety of common commercially available (native and processed) gluten-containing and gluten-free foods and products.

James W Jorgenson - One of the best experts on this subject based on the ideXlab platform.

  • novel aspects of quantitation of immunogenic wheat gluten peptides by liquid chromatography mass spectrometry mass spectrometry
    Journal of Chromatography A, 2010
    Co-Authors: Jennifer A Sealeyvoyksner, Chaitan Khosla, Robert D Voyksner, James W Jorgenson
    Abstract:

    Abstract A novel, specific and sensitive non-immunological liquid chromatography–mass spectrometry (LC–MS) based assay has been developed to detect and quantify trace levels of wheat gluten in food and consumer products. Detection and quantification of dietary gluten is important, because gluten is a principle trigger of a variety of immune diseases including food allergies and intolerances. One such disease, celiac sprue, can cause intestinal inflammation and enteropathy in patients who are exposed to dietary gluten. At present, immunochemistry is the leading analytical method for gluten detection in food. Consequently, enzyme-linked immunosorbent assays (ELISAs), such as the sandwich or competitive type assays, are the only commercially available methods to ensure that food and consumer products are accurately labeled as gluten-free. The availability of a comprehensive, fast and economic alternative to the immunological ELISA may also facilitate research towards the development of new drugs, therapies and food processing technologies to aid patients with gluten intolerances and for gluten-free labeling and certification purposes. LC–MS is an effective and efficient analytical technique for the study of Cereal Grain Proteins and to quantify trace levels of targeted dietary gluten peptides in complex matrices. Initial efforts in this area afforded the unambiguous identification and structural characterization of six unique physiologically relevant wheat gluten peptides. This paper describes the development and optimization of an LC–MS/MS method that attempts to provide the best possible accuracy and sensitivity for the quantitative detection of trace levels of these six peptides in various food and consumer products. The overall performance of this method was evaluated using native Cereal Grains. Experimental results demonstrated that this method is capable of detecting and quantifying select target peptides in food over a range from 10 pg/mg to 100 ng/mg (corresponding to approximately 0.01–100 ppm). Limits of detection (LOD) and quantification (LOQ) for the six target peptides were determined to range from 1 to 30 pg/mg and 10–100 pg/mg respectively. Reproducibility of the assay was demonstrated by evaluation of calibration data as well as data collected from the analysis of quality control standards over a period of four consecutive days. The average coefficient of determination (R2) for each peptide was consistently found to be >0.995 with residuals ranging from approximately 80% to 110%. Spike recovery data for each peptide in various matrices was evaluated at a concentration level near the approximate LOQ for each, as well as at higher concentration levels (30 and 60 ng/mg). The average range of accuracy of detection for all peptides at the lower concentration level was determined to be 90% (±11), while accuracy at the 30 and 60 ng/mg levels was 98% (±5%) and 98% (±3%), respectively. The usefulness and capabilities of this method are presented in a practical application to prospectively screen a variety of common commercially available (native and processed) gluten-containing and gluten-free foods and products.

Chaitan Khosla - One of the best experts on this subject based on the ideXlab platform.

  • novel aspects of quantitation of immunogenic wheat gluten peptides by liquid chromatography mass spectrometry mass spectrometry
    Journal of Chromatography A, 2010
    Co-Authors: Jennifer A Sealeyvoyksner, Chaitan Khosla, Robert D Voyksner, James W Jorgenson
    Abstract:

    Abstract A novel, specific and sensitive non-immunological liquid chromatography–mass spectrometry (LC–MS) based assay has been developed to detect and quantify trace levels of wheat gluten in food and consumer products. Detection and quantification of dietary gluten is important, because gluten is a principle trigger of a variety of immune diseases including food allergies and intolerances. One such disease, celiac sprue, can cause intestinal inflammation and enteropathy in patients who are exposed to dietary gluten. At present, immunochemistry is the leading analytical method for gluten detection in food. Consequently, enzyme-linked immunosorbent assays (ELISAs), such as the sandwich or competitive type assays, are the only commercially available methods to ensure that food and consumer products are accurately labeled as gluten-free. The availability of a comprehensive, fast and economic alternative to the immunological ELISA may also facilitate research towards the development of new drugs, therapies and food processing technologies to aid patients with gluten intolerances and for gluten-free labeling and certification purposes. LC–MS is an effective and efficient analytical technique for the study of Cereal Grain Proteins and to quantify trace levels of targeted dietary gluten peptides in complex matrices. Initial efforts in this area afforded the unambiguous identification and structural characterization of six unique physiologically relevant wheat gluten peptides. This paper describes the development and optimization of an LC–MS/MS method that attempts to provide the best possible accuracy and sensitivity for the quantitative detection of trace levels of these six peptides in various food and consumer products. The overall performance of this method was evaluated using native Cereal Grains. Experimental results demonstrated that this method is capable of detecting and quantifying select target peptides in food over a range from 10 pg/mg to 100 ng/mg (corresponding to approximately 0.01–100 ppm). Limits of detection (LOD) and quantification (LOQ) for the six target peptides were determined to range from 1 to 30 pg/mg and 10–100 pg/mg respectively. Reproducibility of the assay was demonstrated by evaluation of calibration data as well as data collected from the analysis of quality control standards over a period of four consecutive days. The average coefficient of determination (R2) for each peptide was consistently found to be >0.995 with residuals ranging from approximately 80% to 110%. Spike recovery data for each peptide in various matrices was evaluated at a concentration level near the approximate LOQ for each, as well as at higher concentration levels (30 and 60 ng/mg). The average range of accuracy of detection for all peptides at the lower concentration level was determined to be 90% (±11), while accuracy at the 30 and 60 ng/mg levels was 98% (±5%) and 98% (±3%), respectively. The usefulness and capabilities of this method are presented in a practical application to prospectively screen a variety of common commercially available (native and processed) gluten-containing and gluten-free foods and products.

Robert D Voyksner - One of the best experts on this subject based on the ideXlab platform.

  • novel aspects of quantitation of immunogenic wheat gluten peptides by liquid chromatography mass spectrometry mass spectrometry
    Journal of Chromatography A, 2010
    Co-Authors: Jennifer A Sealeyvoyksner, Chaitan Khosla, Robert D Voyksner, James W Jorgenson
    Abstract:

    Abstract A novel, specific and sensitive non-immunological liquid chromatography–mass spectrometry (LC–MS) based assay has been developed to detect and quantify trace levels of wheat gluten in food and consumer products. Detection and quantification of dietary gluten is important, because gluten is a principle trigger of a variety of immune diseases including food allergies and intolerances. One such disease, celiac sprue, can cause intestinal inflammation and enteropathy in patients who are exposed to dietary gluten. At present, immunochemistry is the leading analytical method for gluten detection in food. Consequently, enzyme-linked immunosorbent assays (ELISAs), such as the sandwich or competitive type assays, are the only commercially available methods to ensure that food and consumer products are accurately labeled as gluten-free. The availability of a comprehensive, fast and economic alternative to the immunological ELISA may also facilitate research towards the development of new drugs, therapies and food processing technologies to aid patients with gluten intolerances and for gluten-free labeling and certification purposes. LC–MS is an effective and efficient analytical technique for the study of Cereal Grain Proteins and to quantify trace levels of targeted dietary gluten peptides in complex matrices. Initial efforts in this area afforded the unambiguous identification and structural characterization of six unique physiologically relevant wheat gluten peptides. This paper describes the development and optimization of an LC–MS/MS method that attempts to provide the best possible accuracy and sensitivity for the quantitative detection of trace levels of these six peptides in various food and consumer products. The overall performance of this method was evaluated using native Cereal Grains. Experimental results demonstrated that this method is capable of detecting and quantifying select target peptides in food over a range from 10 pg/mg to 100 ng/mg (corresponding to approximately 0.01–100 ppm). Limits of detection (LOD) and quantification (LOQ) for the six target peptides were determined to range from 1 to 30 pg/mg and 10–100 pg/mg respectively. Reproducibility of the assay was demonstrated by evaluation of calibration data as well as data collected from the analysis of quality control standards over a period of four consecutive days. The average coefficient of determination (R2) for each peptide was consistently found to be >0.995 with residuals ranging from approximately 80% to 110%. Spike recovery data for each peptide in various matrices was evaluated at a concentration level near the approximate LOQ for each, as well as at higher concentration levels (30 and 60 ng/mg). The average range of accuracy of detection for all peptides at the lower concentration level was determined to be 90% (±11), while accuracy at the 30 and 60 ng/mg levels was 98% (±5%) and 98% (±3%), respectively. The usefulness and capabilities of this method are presented in a practical application to prospectively screen a variety of common commercially available (native and processed) gluten-containing and gluten-free foods and products.

Peter R. Shewry - One of the best experts on this subject based on the ideXlab platform.

  • Cereal Grain Proteins
    1996
    Co-Authors: Peter R. Shewry
    Abstract:

    Cereal seed Proteins were among the earliest of all Proteins to be studied, with Beccari (1745) reporting the isolation of wheat gluten. Subsequently Einhof (1805, 1806) reported the first isolation of barley and rye storage Proteins, but it was the pioneering work of T.B. Osborne that placed the study of Cereal Proteins, and other Proteins of plant origin, on a systematic basis. In a series of detailed studies reported between about 1880 and 1920 (see Osborne, 1924) he classified Proteins into groups on the basis of their extraction and solubility in a series of solvents: water (albumins), dilute aqueous salts (globulins), alcohol/ water mixtures (prolamins) and dilute acids or alkalis (glutelins). This has provided a framework for the modern study of Cereal seed Proteins and, indeed, for the classification of Proteins in general.