Occurrence and some properties of trimethylamine-N-oxide demethylase in myofibrillar fraction from walleye pollack muscle.

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The study describes the occurrence and characterization of an enzyme in the myofibrillar fraction from walleye pollack muscle which is responsible for the reduction of trimethylamine-N-oxide to dimethylamine and formaldehyde. The enzyme, trimethylamine-N-oxide demethylase (TMAOase), activity was optimal at pH 7.0-7.5 and was inactivated above 30°C. The apparent activation energy was 30.7 and 55.9 kJ·mol-1·deg-1 above 15°C and in the range of 0-15°C, respectively. Above 0°C, dimethylamine formation increased depending on the rise in temperature, although below 0°C, it slightly increased at -20°C than at 0 and -4°C. The NaCl reduced TMAOase activity at higher concentrations. The enzyme in the myofibrillar fraction required a cofactor system containing Fe2+, ascorbate, and cysteine for full activation.
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