Thiaminase activity was determined for Gulf of Bothnia (GB) and Gulf of Finland (GF) Baltic herring Clupea harengus membras, sprat Sprattus sprattus and three-spined stickleback Gasterosteus aculeatus sampled from either trawl or gillnet catches or from Baltic salmon Salmo salar stomachs. The thiaminase activity in Baltic herring was about 10-fold higher than that in sprat, and there was almost no thiaminase activity in three-spined stickleback. Thiaminase activity of undigested Baltic herring found in Baltic salmon stomachs was significantly higher than that of trawl-caught Baltic herring from the same sea area, suggesting that there may be a higher risk of predation for Baltic herring with high thiaminase activity, possibly linked to their health. Thiaminase activity of the gastrointestinal contents of Baltic salmon, feeding almost entirely on Baltic herring in the GB, was significantly higher than for Baltic salmon feeding on both Baltic herring and sprat in the GF. Therefore, Baltic herring may be the major source of thiaminase for Baltic salmon. A tank experiment demonstrated that thiaminase activity in Baltic herring may vary, even within very short time periods. The results were consistent with the hypothesis that the thiaminase content in Baltic salmon forage fish may be an important link in the aetiology of the thiamine deficiency syndrome, M74, in Baltic salmon.

No abstract

Dietary thiaminase I is a cause of thiamine deficiency in animals. The physiological significance of thiaminase in the organisms containing this enzyme is not known, nor are the factors causing variation in their thiaminase activity. Tests were performed to evaluate the effect a pathogen might have on thiaminase activity in fish, when analyzed both with a cosubstrate added (CATA tests) and no cosubstrate added (NCATA tests). Pyridine is known as a cosubstrate specific for thiaminase I activity that does not accelerate thiaminase II activity. Crucian carp Carassius carassius known to harbor thiaminase I activity were injected intramuscularly with live Aeromonas salmonicida, a pathogenic bacterium of fish. For comparison, other groups were injected with formalin-killed bacteria and phosphate-buffered saline, respectively; an untreated group of fish was kept as a control. The bacteria did not contain any thiaminase activity. Significantly higher thiaminase activities (CATA and NCATA) were measured in all tissues (whole blood, injected muscle, uninjected muscle, and whole fish homogenates) of fish injected with live bacteria than in the saline-injected and the uninjected groups. The thiaminase activity of blood and that in the injected, inflamed muscle tissue followed different allocation patterns in fish injected with live A. salmonicida. The amount of thiaminase I enzyme appeared to be elevated in the whole blood of injected fish in the absence of natural cosubstrate(s). The thiaminase activity of the injected, inflamed muscle suggested that both the amount of thiaminase enzyme and some yet-unidentified natural cosubstrate(s) were elevated. This suggests that in addition to the enzyme, some cosubstrate(s) of fish or pathogen origin play a regulatory role in the so-farunknown physiological significance of thiaminase I activity in vivo. It is suggested that the health of fish should be considered when searching for factor(s) affecting its thiaminase activity.

Potential thiaminase activity of Baltic herring Clupea harengus ranged from 0 to c. 55 nmol g 1 min 1 while potential thiaminase activity in Baltic salmon Salmo salar gastrointestinal (GI) contents ranged from 7 to c. 60 nmol g 1 min 1 . About 30% of the Baltic herring analysed had a potential thiaminase activity equivalent to Baltic salmon GI contents. The results are consistent with the hypothesis that thiaminase in the forage fish of Baltic salmon may be an important link in the aetiology of the thiamine deficiency syndrome, M74, in Baltic salmon and indicate that Baltic salmon might feed selectively on Baltic herring with high thiaminase activity.