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Recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes

The consumption of foods fraught with histamine can lead to various allergy-like symptoms if the histamine is not sufficiently degraded in the human body. The degradation occurs primarily in the small intestine, naturally catalyzed by the human diamine oxidase (DAO). An inherent or acquired deficien...

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Autores principales: Kettner, Lucas, Seitl, Ines, Fischer, Lutz
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9547800/
https://www.ncbi.nlm.nih.gov/pubmed/36208352
http://dx.doi.org/10.1007/s11274-022-03421-2
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author Kettner, Lucas
Seitl, Ines
Fischer, Lutz
author_facet Kettner, Lucas
Seitl, Ines
Fischer, Lutz
author_sort Kettner, Lucas
collection PubMed
description The consumption of foods fraught with histamine can lead to various allergy-like symptoms if the histamine is not sufficiently degraded in the human body. The degradation occurs primarily in the small intestine, naturally catalyzed by the human diamine oxidase (DAO). An inherent or acquired deficiency in human DAO function causes the accumulation of histamine and subsequent intrusion of histamine into the bloodstream. The histamine exerts its effects acting on different histamine receptors all over the body but also directly in the intestinal lumen. The inability to degrade sufficient amounts of dietary histamine is known as the ‘histamine intolerance’. It would be preferable to solve this problem initially by the production of histamine-free or -reduced foods and by the oral supplementation of exogenous DAO supporting the human DAO in the small intestine. For the latter, DAOs from mammalian, herbal and microbial sources may be applicable. Microbial DAOs seem to be the most promising choice due to their possibility of an efficient biotechnological production in suitable microbial hosts. However, their biochemical properties, such as activity and stability under process conditions and substrate selectivity, play important roles for their successful application. This review deals with the advances and challenges of DAOs and other histamine-oxidizing enzymes for their potential application as processing aids for the production of histamine-reduced foods or as orally administered adjuvants to humans who have been eating food fraught with histamine.
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spelling pubmed-95478002022-10-10 Recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes Kettner, Lucas Seitl, Ines Fischer, Lutz World J Microbiol Biotechnol Review The consumption of foods fraught with histamine can lead to various allergy-like symptoms if the histamine is not sufficiently degraded in the human body. The degradation occurs primarily in the small intestine, naturally catalyzed by the human diamine oxidase (DAO). An inherent or acquired deficiency in human DAO function causes the accumulation of histamine and subsequent intrusion of histamine into the bloodstream. The histamine exerts its effects acting on different histamine receptors all over the body but also directly in the intestinal lumen. The inability to degrade sufficient amounts of dietary histamine is known as the ‘histamine intolerance’. It would be preferable to solve this problem initially by the production of histamine-free or -reduced foods and by the oral supplementation of exogenous DAO supporting the human DAO in the small intestine. For the latter, DAOs from mammalian, herbal and microbial sources may be applicable. Microbial DAOs seem to be the most promising choice due to their possibility of an efficient biotechnological production in suitable microbial hosts. However, their biochemical properties, such as activity and stability under process conditions and substrate selectivity, play important roles for their successful application. This review deals with the advances and challenges of DAOs and other histamine-oxidizing enzymes for their potential application as processing aids for the production of histamine-reduced foods or as orally administered adjuvants to humans who have been eating food fraught with histamine. Springer Netherlands 2022-10-08 2022 /pmc/articles/PMC9547800/ /pubmed/36208352 http://dx.doi.org/10.1007/s11274-022-03421-2 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Review
Kettner, Lucas
Seitl, Ines
Fischer, Lutz
Recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes
title Recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes
title_full Recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes
title_fullStr Recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes
title_full_unstemmed Recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes
title_short Recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes
title_sort recent advances in the application of microbial diamine oxidases and other histamine-oxidizing enzymes
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9547800/
https://www.ncbi.nlm.nih.gov/pubmed/36208352
http://dx.doi.org/10.1007/s11274-022-03421-2
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