Liquid Chromatography-Mass Spectrometry Analysis Reveals Hydrolyzed Gluten in Beers Crafted To Remove Gluten

J Agric Food Chem. 2017 Nov 8;65(44):9715-9725. doi: 10.1021/acs.jafc.7b03742. Epub 2017 Oct 30.

Abstract

During brewing, gluten proteins may be solubilized, modified, complexed, hydrolyzed, and/or precipitate. Gluten fragments that persist in conventional beers render them unsuitable for people with celiac disease (CD) or gluten intolerance. Barley-based beers crafted to remove gluten using proprietary precipitation and/or application of enzymes, e.g. prolyl endopeptidases (PEP) that degrade the proline-rich gluten molecules, are available commercially. Gluten measurement in fermented products remains controversial. The industry standard, a competitive ELISA, may indicate gluten values <20 mg/kg, which is deemed safe for people with CD. However, in this study, liquid chromatography-mass spectrometry analyses revealed gluten peptides derived from hydrolyzed fragments, many >30 kDa in size. Barley gluten (hordeins) were detected in all beers analyzed with peptides representing all hordein classes detected in conventional beers but also, alarmingly, in many gluten-reduced beers. It is evident that PEP digestion was incomplete in several commercial beers, and peptides comprising missed cleavages were identified, warranting further optimization of PEP application in an industrial setting.

Keywords: beer; gluten; liquid chromatography−mass spectrometry (LC−MS); prolyl endopeptidase (PEP).

Publication types

  • Evaluation Study

MeSH terms

  • Beer / analysis*
  • Chromatography, Liquid / methods*
  • Glutens / analysis*
  • Hydrolysis
  • Mass Spectrometry / methods*
  • Prolyl Oligopeptidases
  • Serine Endopeptidases / chemistry

Substances

  • Glutens
  • Serine Endopeptidases
  • Prolyl Oligopeptidases