A novel protein glutaminase from Bacteroides helcogenes—characterization and comparison

  • Gudrun Horstmann
  • Jacob Ewert
  • Timo StresslerEmail author
  • Lutz FischerEmail author
Biotechnologically relevant enzymes and proteins


Deamidation is a promising tool to improve solubility and other functional properties of food proteins. One possibility of protein deamidation is the use of a protein glutaminase (PG; EC, an enzyme that catalyzes the deamidation of internal glutamine residues in proteins to glutamic acid residues. The PG from Chryseobacterium proteolyticum is the only one described in literature to date and is commercially available (Amano Enzyme Inc., Japan; PGA). Based on a similarity search, we discovered a predicted, uncharacterized protein from Bacteroides helcogenes and this protein was verified as a PG. After recombinant production and purification, the novel PG (BH-PG) was biochemically characterized and compared with PGA. Some advantageous characteristics for potential application of BH-PG compared with PGA were the higher temperature stability (residual activity after 24 h of incubation at 50 °C was 87% for BH-PG and 2% for PGA), an optimum pH value at acidic conditions (pH 5.5) and less product inhibition by ammonia that is released during the deamidation of proteins (residual activity after adding 40 mM ammonia was 77% for BH-PG and 27% for PGA). Finally, the applicability of BH-PG and PGA was compared by gluten deamidation experiments. Consequently, the final solubility of the nearly insoluble food protein gluten was 94% after BH-PG treatment, whereas the solubility was around 66% when using PGA.


Protein glutaminase Deamidation Solubility increase Gluten 



The authors would like to thank Ines Seitl and Wolfgang Claaßen (University of Hohenheim, Institute of Food Science and Biotechnology, Department of Biotechnology and Enzyme Science) for their help during the molecular biological work and the bioreactor cultivation, respectively.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no competing interests.

Ethical statement

This article does not contain any studies with human participants or animals performed by any of the authors.

Supplementary material

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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Department of Biotechnology and Enzyme Science, Institute of Food Science and BiotechnologyUniversity of HohenheimStuttgartGermany

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