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The temperature and pH repertoire of the transglutaminase family is expanding

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 limi...

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Detalles Bibliográficos
Autores principales: Lerner, Aaron, Ramesh, Ajay, Matthias, Torsten
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7137796/
https://www.ncbi.nlm.nih.gov/pubmed/32170837
http://dx.doi.org/10.1002/2211-5463.12839
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author Lerner, Aaron
Ramesh, Ajay
Matthias, Torsten
author_facet Lerner, Aaron
Ramesh, Ajay
Matthias, Torsten
author_sort Lerner, Aaron
collection PubMed
description 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.
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spelling pubmed-71377962020-04-08 The temperature and pH repertoire of the transglutaminase family is expanding Lerner, Aaron Ramesh, Ajay Matthias, Torsten FEBS Open Bio Commentary 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. John Wiley and Sons Inc. 2020-04-07 /pmc/articles/PMC7137796/ /pubmed/32170837 http://dx.doi.org/10.1002/2211-5463.12839 Text en © 2020 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Commentary
Lerner, Aaron
Ramesh, Ajay
Matthias, Torsten
The temperature and pH repertoire of the transglutaminase family is expanding
title The temperature and pH repertoire of the transglutaminase family is expanding
title_full The temperature and pH repertoire of the transglutaminase family is expanding
title_fullStr The temperature and pH repertoire of the transglutaminase family is expanding
title_full_unstemmed The temperature and pH repertoire of the transglutaminase family is expanding
title_short The temperature and pH repertoire of the transglutaminase family is expanding
title_sort temperature and ph repertoire of the transglutaminase family is expanding
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7137796/
https://www.ncbi.nlm.nih.gov/pubmed/32170837
http://dx.doi.org/10.1002/2211-5463.12839
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