Abstract

Transglutaminases (TGs) play important roles in the food industry, pharmacology, and biotechnology, but as protein cross‐linkers, their complexes are stable, resistant, immunogenic, and potentially pathogenic. Many TGs have been characterized, but they operate in narrow temperature and pH range limits. In a research article in this issue, Clemens Furnes and colleagues describe a novel cold‐adapted TG from Atlantic cod, which expands the operating boundaries to a lower temperature and a wider pH. In this accompanying commentary, we discuss how this TG opens new applications in cold environments and can be deactivated by heating. New sources of TGs should be explored in hot environments like hot springs, in order to increase the temperature and widen the pH ranges for human and industrial benefits.

Highlights

  • The temperature and pH repertoire of the transglutaminase family is expandingKeywords food processing; microbial transglutaminase; pH; temperature; tissue transglutaminase; transglutaminase

  • Characterizing and sequencing the cold Atlantic cod TG (cAcTG) [9] represents a new potential strategy for molecular stable, resistant covalent cross-linking in cold milieu, in the processed food facilities, and in pharmacology, biotechnology, bioconjugation, and antibody– drug conjugates for diagnostic laboratories and medical therapy

  • We hope that the present commentary will encourage the scientific community to explore TG activities in thermophilic bacteria residing in hot springs

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Summary

The temperature and pH repertoire of the transglutaminase family is expanding

Keywords food processing; microbial transglutaminase; pH; temperature; tissue transglutaminase; transglutaminase. Despite the manufacturer’s claims of being safe and it being categorized as GRAS (generally recognized as safe), its cross-linked gliadin complexes were recently shown to be immunogenic and potentially pathogenic in CD [5,6,7] This was a topic of criticism as it was assumed that no active mTG reached the human intestinal lumen, due to its industrial temperature inactivation and inability to resist the gastric acidic pH [8]. In this regard, Alvarez et al should be congratulated for addressing the topic of temperature and pH dependency of TG, by characterizing a novel cold-adapted TG enzyme and indicating its potential application for medicine and food processing, as described in a research article published. We discuss the features of cold Atlantic cod TG (cAcTG) temperature and pH dependency with relation to the need of processed food manufacturers for more adapted TGs that will operate under more extreme temperatures and pH environments

Human gut lumen sources of transglutaminases
Processed food additive Pathobionts Probiotics Plants Vegetables Meat
Summary
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