Evaluation of histidine decarboxylase activity of bacteria isolated from sardine (Sardina pilchardus) by an enzymic method

E. I. López‐Sabater; J. J. Rodriguez‐Jerez; M. Hernández‐Herrero; M. T. Mora‐Ventura

doi:10.1111/j.1472-765X.1994.tb00908.x

Evaluation of histidine decarboxylase activity of bacteria isolated from sardine (Sardina pilchardus) by an enzymic method

E. I. López‐Sabater, J. J. Rodriguez‐Jerez, M. Hernández‐Herrero, M. T. Mora‐Ventura

Department of Animal and Food Science

Research output: Contribution to journal › Article › Research › peer-review

58 Citations (Scopus)

Abstract

A fast and simple enzymic method has been adapted to measure histidine decarboxylase activity in bacteria isolated from fish. It was possible to quantify the presence of histamine at levels higher than 1.03 times 10‐2μmol (3 ppm) per ml of culture medium. There was a good correlation (γ=0.99) between the histamine content and the increase of absorbance in the concentration range of 3 and 30 ppm. The method can be used for quantitation of the amount of histamine produced by a selected strain, and has the advantages of being low in cost, reliable, easy to use and fast to perform. Plesiomonas shigelloides, a bacterium frequently isolated from fish and aquatic environments, has been identified as a new histamine‐former in fish. Copyright © 1994, Wiley Blackwell. All rights reserved

Original language	English
Pages (from-to)	70-75
Journal	Letters in Applied Microbiology
Volume	19
Issue number	2
DOIs	https://doi.org/10.1111/j.1472-765X.1994.tb00908.x
Publication status	Published - 1 Jan 1994

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title = "Evaluation of histidine decarboxylase activity of bacteria isolated from sardine (Sardina pilchardus) by an enzymic method",

abstract = "A fast and simple enzymic method has been adapted to measure histidine decarboxylase activity in bacteria isolated from fish. It was possible to quantify the presence of histamine at levels higher than 1.03 times 10‐2μmol (3 ppm) per ml of culture medium. There was a good correlation (γ=0.99) between the histamine content and the increase of absorbance in the concentration range of 3 and 30 ppm. The method can be used for quantitation of the amount of histamine produced by a selected strain, and has the advantages of being low in cost, reliable, easy to use and fast to perform. Plesiomonas shigelloides, a bacterium frequently isolated from fish and aquatic environments, has been identified as a new histamine‐former in fish. Copyright {\textcopyright} 1994, Wiley Blackwell. All rights reserved",

author = "L{\'o}pez‐Sabater, {E. I.} and Rodriguez‐Jerez, {J. J.} and M. Hern{\'a}ndez‐Herrero and Mora‐Ventura, {M. T.}",

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Evaluation of histidine decarboxylase activity of bacteria isolated from sardine (Sardina pilchardus) by an enzymic method. / López‐Sabater, E. I.; Rodriguez‐Jerez, J. J.; Hernández‐Herrero, M.; Mora‐Ventura, M. T.

In: Letters in Applied Microbiology, Vol. 19, No. 2, 01.01.1994, p. 70-75.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - Evaluation of histidine decarboxylase activity of bacteria isolated from sardine (Sardina pilchardus) by an enzymic method

AU - López‐Sabater, E. I.

AU - Rodriguez‐Jerez, J. J.

AU - Hernández‐Herrero, M.

AU - Mora‐Ventura, M. T.

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AB - A fast and simple enzymic method has been adapted to measure histidine decarboxylase activity in bacteria isolated from fish. It was possible to quantify the presence of histamine at levels higher than 1.03 times 10‐2μmol (3 ppm) per ml of culture medium. There was a good correlation (γ=0.99) between the histamine content and the increase of absorbance in the concentration range of 3 and 30 ppm. The method can be used for quantitation of the amount of histamine produced by a selected strain, and has the advantages of being low in cost, reliable, easy to use and fast to perform. Plesiomonas shigelloides, a bacterium frequently isolated from fish and aquatic environments, has been identified as a new histamine‐former in fish. Copyright © 1994, Wiley Blackwell. All rights reserved

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DO - 10.1111/j.1472-765X.1994.tb00908.x

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