Thiaminase from Fresh-Water, Brackish-Water and Salt-Water Fish

Deolalkar, S.T.; Sohonie, K.

doi:10.1038/173489a0

Cited by 15 publications

(9 citation statements)

References 3 publications

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“…The true source of thiaminase activity in aquatic ecosystems remains elusive. Potential sources that merit further investigation include non-P. thiaminolyticus bacteria, de novo synthesis by lower trophic-level food items such as zooplankton or mussels, and de novo synthesis of thiaminase by fishes (Deolalkar and Sohonie 1954;Boś and Kozik 2000;Nishimune et al 2008). Many potential bacterial sources of thiaminase activity exist, and comparing the composition of the bacterial flora in fish viscera with and withou thiaminase activity would be useful for determining if particular bacterial species are associated with increased thiaminase activity.…”

Section: Discussionmentioning

confidence: 99%

Paenibacillus thiaminolyticus is not the cause of thiamine deficiency impeding lake trout (Salvelinus namaycush) recruitment in the Great Lakes

Richter

Evans

Wright-Osment

et al. 2012

Can. J. Fish. Aquat. Sci.

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Thiamine (vitamin B1) deficiency is a global concern affecting wildlife, livestock, and humans. In Great Lakes salmonines, thiamine deficiency causes embryo mortality and is an impediment to restoration of native lake trout ( Salvelinus namaycush ) stocks. Thiamine deficiency in fish may result from a diet of prey with high levels of thiaminase I. The discoveries that the bacterial species Paenibacillus thiaminolyticus produces thiaminase I, is found in viscera of thiaminase-containing prey fish, and causes mortality when fed to lake trout in the laboratory provided circumstantial evidence implicating P. thiaminolyticus. This study quantified the contribution of P. thiaminolyticus to the total thiaminase I activity in multiple trophic levels of Great Lakes food webs. Unexpectedly, no relationship between thiaminase activity and either the amount of P. thiaminolyticus thiaminase I protein or the abundance of P. thiaminolyticus cells was found. These results demonstrate that P. thiaminolyticus is not the primary source of thiaminase activity affecting Great Lakes salmonines and calls into question the long-standing assumption that P. thiaminolyticus is the source of thiaminase in other wild and domestic animals.

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Section: Discussionmentioning

confidence: 99%

Paenibacillus thiaminolyticus is not the cause of thiamine deficiency impeding lake trout (Salvelinus namaycush) recruitment in the Great Lakes

Richter

Evans

Wright-Osment

et al. 2012

Can. J. Fish. Aquat. Sci.

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“…Early studies measured thiaminase activity by assaying the disappearance of thiamine in the presence of biological tissues, typically from fish [25], [26], [30]. Several alternative methods were developed [31], [32] before Edwin and Jackman [4] laid the foundation for a radiometric thiaminase assay that was used extensively for the next 40 years (see [18], [33], [34] for subsequent modifications of this method).…”

Section: Introductionmentioning

confidence: 99%

A Rapid Method for Assaying Thiaminase I Activity in Diverse Biological Samples

2014

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Vitamin B1 (thiamine) deficiencies can lead to neurological disorders, reproductive failure and death in wild and domestic animal populations. In some cases, disease is brought about by the consumption of foods high in thiaminase I activity. Levels of thiaminase activity in these foods are highly variable and the factors leading to production of this enzyme are poorly understood. Here we describe improvements in a spectrophotometric thiaminase I activity assay that measures the disappearance of 4-nitrothiophenol, a favored nucleophile co-substrate that replaces the thiazole portion of thiamine during the inactivation of thiamine by the enzyme. Scalable sample processing protocols and a 96-well microtiter plate format are presented that allow the rapid evaluation of multiple, replicated samples in the course of only a few hours. Observed levels of activity in bacterial culture supernatant, fish, ferns and molluscs using this colorimetric assay were similar to previously published reports that employed a radiometric method. Organisms devoid of thiaminase I, based upon previous work, showed no activity with this assay. In addition, activity was found in a variety of fishes and one fern species from which this enzyme had not previously been reported. Overall, we demonstrate the suitability of this technique for measuring thiaminase I activity within small amounts of tissue and environmental samples with replication levels that were heretofore prohibitive. The assay provides a considerable improvement in the ability to examine and understand the properties of an enzyme that has a substantial influence on organism and ecosystem health.

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“…Thiaminase has been found in some Indian salt water and brackish water fish. [18] Betel nut has also been shown to possess antithiamine activity. [19] Both fish and betel nut are consumed widely in this region.…”

mentioning

confidence: 99%