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Original Articles

Updated Molecular Knowledge about Histamine Biosynthesis by Bacteria

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Pages 697-714 | Published online: 28 Aug 2008
 

Abstract

Histamine poisoning is caused by the ingestion of food containing high levels of histamine, a biogenic amine. Histamine could be expected in virtually all foods that contain proteins or free histidine and that are subject to conditions enabling microbial activity. In most histamine-containing foods the majority of the histamine is generated by decarboxylation of the histidine through histidine decarboxylase enzymes derived from the bacteria present in food. Bacterial histidine decarboxylases have been extensively studied and characterized in different organisms and two different enzymes groups have been distinguished, pyridoxal phosphate- and the pyruvoyl-dependent. Pyridoxal phosphate-dependent histidine decarboxylases are encountered in Gram-negative bacteria belonging to various species. Pyruvoyl-dependent histidine decarboxylases are found in Gram-positive bacteria and specially in lactic acid bacteria implicated in food fermentation or spoilage. The molecular organization of the genes involved in histamine production have been elucidated in several histamine-producer bacteria. This molecular knowledge has led to the development of molecular methods for the rapid detection of bacteria possessing the ability to produce histamine. The detection of histamine-producer bacteria is of great importance for its potential health hazard as well as from an economic point of view since products exceeding recommended limits can be refused in commercial transactions.

ACKNOWLEDGEMENTS

This work was supported by grants AGL2005-00470, AGL2008-01052, and FUN-C-FOOD Consolider 25506 (CICYT), RM2008-002 (INIA), and S-0505/AGR/000153 (CAM). We are grateful to M. V. Santamaría. J. M. Landete is a recipient of a postdoctoral fellowship from the MEC.

Notes

* Plasmid encoded histidine decarboxylase.

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