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Heppenheim an der Bergstrasse, Germany

Haas-Lauterbach S.,R Biopharm
Journal of AOAC International | Year: 2012

The second generation of a competitive ELISA for prolamin quantification based on the R5 antibody was studied for method performance and suitability to detect partially hydrolyzed prolamins in food. To be able to convert signal intensities to gluten concentrations, as required by the Codex Alimentarius Standard, a new calibrator consisting of a peptic-tryptic digest of wheat, rye, and barley prolamins was used for the first time. LOD and LOQ of the assay were 1.36 and 5.0 mg prolamin/kg food, respectively. Analysis of beer samples and a hydrolyzed wheat product showed that the assay provided significantly higher prolamin concentrations, compared to the sandwich ELISA based on the same antibody, which is only suitable for the detection of intact prolamins. Spiking experiments with defined concentrations of partially hydrolyzed prolamins gave recoveries ranging from 92 to 136%. Source


Haas-Lauterbach S.,R Biopharm | Immer U.,R Biopharm | Richter M.,R Biopharm | Koehler P.,German Research Center for Food Chemistry
Journal of AOAC International | Year: 2012

The second generation of a competitive ELISA for prolamin quantification based on the R5 antibody was studied for method performance and suitability to detect partially hydrolyzed prolamins in food. To be able to convert signal intensities to gluten concentrations, as required by the Codex Alimentarius Standard, a new calibrator consisting of a peptic-tryptic digest of wheat, rye, and barley prolamins was used for the first time. LOD and LOQ of the assay were 1.36 and 5.0 mg prolamin/ kg food, respectively. Analysis of beer samples and a hydrolyzed wheat product showed that the assay provided significantly higher prolamin concentrations, compared to the sandwich ELISA based on the same antibody, which is only suitable for the detection of intact prolamins. Spiking experiments with defined concentrations of partially hydrolyzed prolamins gave recoveries ranging from 92 to 136%. © 2012 Publishing Technology. Source


Lacorn M.,R Biopharm | Goerke M.,University of Hohenheim | Claus R.,University of Hohenheim
Journal of Animal Physiology and Animal Nutrition | Year: 2010

Carbohydrates, which were not digested in the jejunum, will be fermented by micro-organisms to short chain fatty acids. These are transported by the monocarboxylate transporter 1 (MCT1) through the gut wall and serve as fuels for colonic cells. To deliver butyrate to the distal part of the intestine, inulin with a low precaecal digestibility was chosen as a coating material. Approximately 150 g of inulin-coated butyrate (containing 81 g butyrate) per day was fed to pigs (mean weight: 97 kg) over a period of 6 days after an adaptation period of 6 days with linear increasing amounts of butyrate. The following observations compared to controls were observed: (1) coating was digested microbially in the ileum; (2) MCT1-mRNA showed a higher expression in the ileum; (3) apoptosis was reduced in the ileum but mitosis was not changed; and (4) length of villi increased by approximately 25% in the ileum. Feeding inulin-coated butyrate resulted in an increased ileal surface. Delivery of butyrate to the colon requires a more resistant inulin-coating. © 2009 Blackwell Verlag GmbH. Source


Olling A.,R Biopharm | Leidinger H.,R Biopharm | Hoffmann R.,Institute For Labormedizin Und Mikrobiologie
European Journal of Clinical Microbiology and Infectious Diseases | Year: 2016

To compare Clostridium. (C.) difficile toxin A/B and glutamate dehydrogenase (GDH) enzyme immunoassays or rapid diagnostic tests to toxinogenic culture on recently described highly selective agar plates. Five hundred consecutive samples sent in for C. difficile diagnostics were tested by toxin A/B enzyme immunoassay (EIA) and rapid diagnostic test (RDT), GDH EIA and RDT, and culture on chromID C. difficile plates for 48 hrs, with toxin testing from culture if the toxin EIA from feces was negative. Samples with discordant results from EIA and RDT were submitted to C. difficile-specific 16S rRNA gene and tcdB PCR. Ninety-two, 88, 31, and 37 samples were positive by GDH EIA, GDH RDT, toxin A/B EIA, and toxin A/B RDT respectively. Seventy-four samples were positive by culture, 54 culture-positive samples were subjected to repeat toxin testing, with an additional 29 samples positive. Thus, there were 60 C. difficile toxin A/B positive samples in total (12 %). Single-step screening with GDH EIA, GDH RDT, toxin A/B EIA, and toxin A/B RDT would have missed seven (12 %), 11 (18 %), 29 (48 %) or 27 (45 %) of all positive samples respectively. Single-step screening with GDH or toxin A/B tests from feces misses a significant proportion of patients compared to toxinogenic culture, putting these patients at risk from undiagnosed C. difficile infection. More data are needed to establish the clinical significance of a positive toxinogenic culture result in the absence of detectable toxin A/B in feces. © 2016 Springer-Verlag Berlin Heidelberg Source


Pajestka M.,Albert Ludwigs University of Freiburg | Muller H.,Sensovation AG | Ait-Benarrou A.,R Biopharm | Brandstetter T.,Albert Ludwigs University of Freiburg | Ruhe J.,Albert Ludwigs University of Freiburg
BioSpektrum | Year: 2013

Not many microfluidic diagnostic platforms reached commercialization so far. Sample-to-answer systems are required for that. Here, we are presenting in brief a microarray-based multi parametric analysis system for proteins related to allergy in microtiter plates using a highly sensitive, easy-to-use reader system. For improved sensitivity and to obtain a high signal-to-background ratio, proteins were immobilized with a new 3D-hydrogel technology. © 2013 Springer-Verlag Berlin Heidelberg. Source

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