Production of the prolyl endoprotease (PEP) from Aspergillus sp. FSDE 16 by solid-state fermentation (SSF) and use for producing a gluten-free beer

Biotechnol Appl Biochem. 2024 Apr;71(2):460-476. doi: 10.1002/bab.2552. Epub 2024 Jan 11.

Abstract

Beer is a beverage that contains gluten and cannot be consumed by people with celiac disease. In this context, the enzyme prolyl endoprotease (PEP) can be used to reduce the gluten content in beer. The present study aimed to produce the PEP from Aspergillus sp. FSDE 16 using solid-state fermentation with 5 conditions and comparing with a similar commercial enzyme produced from Aspergillus niger in the production of a gluten-free beer. The results of the performed cultures showed that during the culture, the most increased protease activity (54.46 U/mL) occurred on the 4th day. In contrast, for PEP, the highest activity (0.0356 U/mL) was obtained on the 3rd day of culture in condition. Regarding beer production, cell growth, pH, and total soluble solids showed similar behavior over the 7 days for beers produced without enzyme addition or with the addition of commercial enzyme and with the addition of the enzyme extract produced. The addition of the enzyme and the enzyme extract did not promote changes, and all the beers produced showed similar and satisfactory results, with acid pH between 4 and 5, total soluble solids ranging from 4.80 to 5.05, alcohol content ranging from 2.83% to 3.08%, and all beers having a dark character with deep amber and light copper color. Gluten removal was effectively using the commercial enzyme and the enzyme produced according to condition (v) reaching gluten concentrations equal to 17 ± 5.31 and 21.19 ± 11.28 ppm, respectively. In this way, the production of the enzyme by SSF and its application in the removal of gluten in beer was efficient.

Keywords: beer; celiac disease; craft beer; gluten; prolyl endoprotease (PEP).

MeSH terms

  • Aspergillus niger
  • Beer* / analysis
  • Fermentation
  • Glutens / analysis
  • Glutens / metabolism
  • Humans
  • Plant Extracts
  • Prolyl Oligopeptidases
  • Serine Endopeptidases* / chemistry
  • Serine Endopeptidases* / metabolism

Substances

  • Serine Endopeptidases
  • Prolyl Oligopeptidases
  • Glutens
  • Plant Extracts