Solubilization of gliadins for use as a source of nitrogen in the selection of bacteria with gliadinase activity. (1st February 2015)

• Record Type: Journal Article
• Authors: Alvarez-Sieiro, Patricia; Redruello, Begoña; Ladero, Victor; Cañedo, Elena; Martin, M. Cruz; Fernández, María; Alvarez, Miguel A.
• Is Part Of: Food chemistry. Volume 168(2015)
• Page Start: 439
• Page End: 444
• Publication Date: 2015-02-01
• Subjects: Gluten -- Gliadin solubility -- Gliadinase -- Culture medium -- Zymography; Gliadin (PubChem CID: 17787981) -- Diethyl ethoxymethylenemalonate (PubChem CID: 6871) -- Azocasein (PubChem CID: 39859) -- Cycloheximide (PubChem CID: 6197); Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2014.07.085
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Gliadin, solubilized by mild acid treatment was used as nitrogen source in a culture medium. Acid hydrolyzed gliadin is a reliable substrate in gliadinase detection. An acid hydrolyzed gliadin based medium selected bacteria with gliadinase activity. Zymographic separation of gliadinases produced by bacteria was achieved in the study. Abstract: 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.