For patients with celiac disease, gliadin detoxification via the use of gliadinases may provide an alternative to a gluten-free diet. A culture medium, in which gliadins were the sole source of nitrogen, was developed for screening for microorganisms with gliadinase activity. The problem of gliadin insolubility was solved by mild acid treatment, which renders an acid-hydrolysed gliadin/peptide mixture (AHG). This medium provided a sensitive and reliable means of detecting proteases, compared to the classical spectrophotometric method involving azocasein. When a sample of fermented wheat (a source of bacteria) was plated on an AHG-based culture medium, strains with gliadinase activity were isolated. These strains' gliadinase profiles were determined using an AHG-based substrate in zymographic analyses.
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http://dx.doi.org/10.1016/j.foodchem.2014.07.085 | DOI Listing |
Food Res Int
December 2023
Department of Microbiology, Central University of Haryana, Mahendergarh 123031, India. Electronic address:
The present study reported the characterization of gluten hydrolyzing strains of Bacillus sp. from fermented cereal dough. The strains were characterized for probiotic as well as technological attributes.
View Article and Find Full Text PDFJ Agric Food Chem
November 2023
Graduate Institute of Biotechnology, National Chung Hsing University, 250 Kuo-Kuang Road, Taichung 40227, Taiwan.
An aspartate peptidase with proteolytic activity toward gluten was identified from an isolated red yeast strain. This peptidase consists of 425 amino acids, comprising an N-terminal signal peptide, a propeptide, and a C-terminal catalytic domain. The catalytic domain, termed RmuAP1, could be secreted by the recombinant oleaginous yeast , whose genome contains the expression cassette for RmuAP1.
View Article and Find Full Text PDFInt J Mol Sci
October 2020
Área de Bioquímica y Biología Molecular, Departamento de Biología Molecular, Facultad de Veterinaria, Universidad de León, 24071 León, Spain.
The human gastrointestinal system has the capacity to metabolize dietary gluten. The capacity to degrade gliadin-derived peptide is present in humans from birth and increases during the first stages of life (up to 6-12 months of age). Fecal samples from 151 new-born and adult non-celiac disease (NCD) volunteers were collected, and glutenase and glianidase activities were evaluated.
View Article and Find Full Text PDFMol Metab
July 2017
Departamento de Biología Molecular, Área de Bioquímica y Biología Molecular, Universidad de León, Facultad de Veterinaria, 24071 León, Spain.
Objective: To identify, purify, and characterize the proteins responsible for glutenase activity in the feces of healthy subjects and patients with celiac disease (CD).
Methods: Sixteen subjects were included in this study; 8 were healthy with no known food intolerances, and 8 were treated CD patients on a gluten-free diet. Fecal samples were homogenized, and precipitated proteins were purified by chromatography.
Food Chem
February 2015
Dairy Research Institute (IPLA-CSIC), 33300 Villaviciosa, Asturias, Spain. Electronic address:
For patients with celiac disease, gliadin detoxification via the use of gliadinases may provide an alternative to a gluten-free diet. A culture medium, in which gliadins were the sole source of nitrogen, was developed for screening for microorganisms with gliadinase activity. The problem of gliadin insolubility was solved by mild acid treatment, which renders an acid-hydrolysed gliadin/peptide mixture (AHG).
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