Effect of trimethylamine-N-oxide demethylase from lizardfish kidney on biochemical changes of haddock natural actomyosin stored at 4 and -10 °C
2008
Leelapongwattana, Kittima | Benjakul, Soottawat | Visessanguan, Wonnop | Howell, Nazlin K
The addition of partially purified trimethylamine-N-oxide demethylase (TMAOase) from lizardfish kidney to haddock natural actomyosin (NAM) in the presence of cofactors (FeCl₂, ascorbate, and cysteine) accelerated formaldehyde (FA) formation throughout the storage either at 4 or -10 °C (p < 0.05). ¹H NMR spectroscopic study revealed that the formation of dimethylamine was enhanced with a concomitant decrease in trimethylamine oxide (TMAO) content when TMAOase was added, particularly at higher concentration. The loss of protein solubility increased as the result of FA formation, which was associated with the increased denaturation/aggregation of proteins. Lipid oxidation determined as hexanal content occurred during extended storage at different degrees. Generally, simulated systems without TMAOase and TMAO contained the highest hexanal content. Differential scanning calorimetry of NAM after storage at 4 and -10 °C for 15 days and for 8 weeks, respectively, showed the lower T m and enthalpy of endothermic peaks corresponding to myosin and actin, suggesting the conformational changes induced by FA formed. Therefore, TMAOase exhibited the detrimental impact on haddock NAM, mainly caused by FA formation.
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